Updated November 6, 1996

This bibliography of Optima XL-A applications is arranged by subject categories, then by first author within the subject groups. The eleven subject categories are: Binding Studies and Complexes; General Studies; Glycoproteins and Proteoglycans; Lipoproteins; Miscellaneous Samples (Including Peptides); Nucleic Acids; Proteins: Enzymes; Proteins: Receptors; Proteins: Other Proteins; Synthetic Polymers; Viruses. Some references may appear in more than one category. In addition, each time the bibliography is updated, the added references will appear also in the NEW section on the first page.

Each reference is followed by a brief annotation that summarizes some of the Optima XL-A experimental detail and includes the address of one of the authors. The General Studies category contains references to theory, methods, and instrumentation of interest, which frequently do not include any experimental description.

NEW: The following thirteen recently published references have been added since the

October 1, 1996 bibliography update.

**Boice, J. A., Fairman, R. Structural characterization of the tumor suppressor p16, an ankyrin-like repeat protein. Protein Sci. 5, 1776-1784 (1996)

Optima XL-A, sed. equil., M(r), state of association; recombinant human tumor suppressor p16 monomer-dimer; An-60 Ti, 15, 20, 25 and 35 krpm; 239 and 280 nm, 4deg.C; CD and fluorescence also used; effect of concentration; (Fairman) Div. of Macromolecular Structure, Bristol-Myers Squibb Pharmaceutical Research Inst., P. O. Box 4000, Princeton, NJ 08543-4000

**Cabral, J. H. M., Petosa, C., Sutcliffe, M. J., Raza, S., Byron, O., Poy, F., Marfatia, S. M., Chishti, A. H., Liddington, R. C. Crystal structure of a PDZ domain. Nature 382, 649-652 (1996)

Optima XL-A, sed. equil., K(d), m; recombinant human Dlg protein PDZ-3 dimer; 30 krpm, 220 and 278 nm, 20deg.C; X-ray crystallography also used; Dept. of Biochemistry, NCMH and Chemistry, Univ. of Leicester, Leicester LE1 7RH, UK

**Calvert, R., Kahana, E., Gratzer, W. B. Stability of the dystrophin rod domain fold: evidence for nested repeating units. Biophys. J. 71, 1605-1610 (1996)

Optima XL-A, sed. equil., M; sed. vel., S; recombinant human dystrophin fragments; 24 and 28 krpm, then 42 krpm (s.e.), 42 or 60 krpm (s.v.); 230 and 280 nm, 5 or 10deg.C; CD and PAGE also used; (Gratzer) MRC Muscle and Cell Motility Unit, King's College, 26-29 Drury Lane, London WC2B 5RL, UK

**Colfen, H., Harding, S. E., Boulter, J. M., Watts, A. Hydrodynamic examination of the dimeric cytoplasmic domain of the human erythrocyte anion transporter, band 3. Biophys. J. 71, 1611-1615 (1996)

Optima XL-A, sed. equil., K(d), M(w); sed. vel., S; human erythrocyte band 3 protein cytoplasmic domain; 10 krpm (s.e.); 3, 5, 10, 15 and 40 krpm (s.v.); 280 nm, 20deg.C; Model E with interference optics used to compare sed. equil. data with XL-A; gel filtration also used; effect of concentration and speed; (Harding) Natl. Centre for Macromolecular Hydrodynamics, Univ. of Nottingham, Sutton Bonington LE12 5RD, UK

**Consalvi, V., Chiaraluce, R., Millevoi, S., Pasquo, A., Vecchini, P., Chiancone, E., Scandurra, R. Refolding pathway and association intermediates of glutamate dehydrogenase from the hyperthermophile Pyrococcus furiosus. Eur. J. Biochem. 239, 679-685 (1996)

Optima XL-A, sed. vel., S; Pyrococcus furiosus glutamate dehydrogenase and oligomers; 30 or 40 krpm, 280 nm, 20deg.C; CD, fluorescence, light scattering and SEC also used; Dipartimento di Scienze Biochimiche 'A. Rossi Fanelli', Universita 'La Sapienza', Piazzale Aldo Moro, 5, I-00185 Roma, Italy

**Easa, A. M., Armstrong, H. J., Mitchell, J. R., Hill, S. E., Harding, S. E., Taylor, A. J. Maillard induced complexes of bovine serum albuminña dilute solution study. Int. J. Biol. Macromol. 18, 297-301 (1996)

Optima XL-A, sed. vel., S, m estimated from S and D (determined by light scattering); bovine serum albumin aggregates; 15-40 krpm, 280 nm, 20deg.C; albumin heated at 95deg.C between 10 and 80 min with and without the presence of xylose; (Hill) Univ. of Nottingham, Dept. of Applied Biochemistry and Food Science, Sutton Bonington Campus, Loughborough, LE12 5RD, UK

**Faix, J., Steinmetz, M., Boves, H., Kammerer, R. A., Lottspeich, F., Mintert, U., Murphy, J., Stock, A., Aebi, U., Gerisch, G. Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail. Cell 86, 631-642 (1996)

Optima XL-A, sed. equil., M(r); sed. vel., S; recombinant Dictyostelium discoideum cortexillin I dimer; 12 krpm (s.e.), 56 krpm (s.v.), 230 nm, 20deg.C; CD and electron microscopy also used; Max-Planck-Institut fur Biochemie D-82152 Martinsried, Federal Republic of Germany

**Kojima, S., Kuriki, Y., Sato, Y., Arisaka, F., Kumagai, I., Takahashi, S., Miura, K. Synthesis of alpha-helix-forming peptides by gene engineering methods and their characterization by circular dichroism spectra measurements. Biochim. Biophys. Acta 1294, 129-137 (1996)

Optima XL-A, sed. equil., M, state of oligomerization; recombinant alpha-helix-forming peptides; An-60 Ti, 20 krpm, 230 nm, 20deg.C; CD and gel filtration also used; state of oligomerization; (Miura) Inst. for Biomolecular Science, Gakushuin Univ., Mejiro, Tokyo 171, Japan

**Kosukegawa, A., Arisaka, F., Takayama, M., Yajima, H., Kaidow, A., Handa, H. Purification and characterization of virus-like particles and pentamers produced by the expression of SV40 capsid proteins in insect cells. Biochim. Biophys. Acta 1290, 37-45 (1996)

Optima XL-A, sed. equil., m; sed. vel., S; recombinant baculovirus-expressed SV40 virus-like particles and capsid protein pentamers; An-60 Ti, 3500 rpm (s.e.), 10, 15, or 40 krpm (s.v.), 20deg.C, 280 nm; electron microscopy also used; (Handa) Faculty of Bioscience and Biotechnology, Tokyo Inst. of Technology, 4259 Nagatsuta-cho, Midori-ku Yokohama 226, Japan

**Mouz, N., Tricot, C., Ebel, C., Petillot, Y., Stalon, V., Dideberg, O. Use of a designed fusion protein dissociates allosteric properties from the dodecameric state of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. Proc. Natl. Acad. Sci. 93, 9414-9419 (1996)

Optima XL-A, sed. equil., m; sed. vel., S; recombinant bacterial ornithine carbamoyltransferase; An-60 Ti, 10 krpm (s.e.), 30 krpm (s.v.), 10deg.C; gel filtration and PAGE also used; (Dideberg) Laboratoire de Cristallographie Macromoleculaire, Institut de Biologie Structurale Jean-Pierre EBEL, Commissariat a l'Energie Atomique-Centre National de la Recherche Scientifique, 41 avenue des Martyrs, F-38027 Grenoble Cedex 1, France

**Narhi, L. O., Philo, J. S., Li, T., Zhang, M., Samal, B., Arakawa, T. Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: thermal and trifluoroethanol-induced denaturation at neutral pH. Biochemistry 35, 11447-11453 (1996)

Optima XL-A, sed. equil., state of association; recombinant human or murine tumor necrosis factor-alpha monomer-trimer; 10, 14 and 20 krpm, 230 or 280 nm, 25deg.C; effect of concentration; CD also used; Amgen Inc., Amgen Center, M/S 14-2-D, Thousand Oaks, CA 91320-1789

**Narhi, L. O., Philo, J. S., Li, T., Zhang, M., Samal, B., Arakawa, T. Induction of alpha-helix in the beta-sheet protein tumor necrosis factor-alpha: acid-induced denaturation. Biochemistry 35, 11454-11460 (1996)

Optima XL-A, sed. vel., D, g(s*), M(r), S; recombinant human or murine tumor necrosis factor-alpha monomer-trimer; 60 krpm, 230 nm, 20deg.C; effect of pH; CD and FTIR also used; Amgen Inc., Amgen Center, M/S 14-2-D, Thousand Oaks, CA 91320-1789

**Truckses, D. M., Somoza, J. R., Prehoda, K. E., Miller, S. C., Markley, J. L. Coupling between trans/cis proline isomerization and protein stability in staphylococcal nuclease. Protein Sci. 5, 1907-1916 (1996)

Optima XL-A, sed. equil., state of association; recombinant bacterial mutant nucleases; 25, 33 and 37 krpm; 280 nm; NMR and X-ray crystallography also used; (Markley) Dept. of Biochemistry, College of Agricultural and Life Sciences, Univ. of Wisconsin-Madison, 420 Henry Mall, Madison, WI 53706

Binding Studies and Complexes

**Arakawa, T., Philo, J., Kenney, W. C. Structure and solubility of interleukin-2 in sodium dodecyl sulfate. Int. J. Pept. Protein Res. 43, 583-587 (1994)

Optima XL-A, sed. vel., S; recombinant interleukin-2ñSDS complexes; 30 & 60 krpm; 215 nm or 280 nm; effect of SDS concentration; Amgen Inc., Amgen Center, Thousand Oaks, CA

**Arakawa, T., Haniu, M., Narhi, L. O., Miller, J. A., Talvenheimo, J., Philo, J. S., Chute, H. T., Matheson, C., Carnahan, J., Louis, J.-C., Yan, Q., Welcher, A. A., Rosenfeld, R. Formation of heterodimers from three neurotrophins, nerve growth factor, neurotrophin-3, and brain-derived neurotrophic factor. J. Biol. Chem. 269, 27833-27839 (1994)

Optima XL-A, sed. equil., m, state of association; neurotrophin-3ñbrain-derived neurotrophic factor heterodimer; 20-48 krpm, effect of conc.; CD also; Amgen Inc., Thousand Oaks, CA 91320-1789

**Balagurumoorthy, P., Sakamoto, H., Lewis, M. S., Zambrano, N., Clore, G. M., Gronenborn, A. M., Appella, E., Harrington, R. E. Four p53 DNA-binding domain peptides bind natural p53-response elements and bend the DNA. Proc. Natl. Acad. Sci. 92, 8591-8595 (1995)

Optima XL-A, sed. equil., binding stoichiometry, K(d); p53 DNA-binding domain peptidesóDNA complexes; 16 krpm, multiwavelength scanning method, 20deg.C; (Harrington) Dept. of Biochemistry, Univ. of Nevada Reno, Reno, NV 89557-0014

**Behlke, J., Ristau, O., Marg, A. Complex formation and crystallization of adrenodoxin-reductase with adrenodoxin. Progress in Colloid & Polymer Science, Vol. 99, pp. 63-68. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A, sed. equil., K(a), m; adrenodoxin-adrenodoxin reductase interaction; 20 and 24 krpm; 378, 415 and 450 nm or 230, 235 and 240 nm; effect of concentration and ionic strength; 10deg.C; Max Delbruck Center for Molecular Medicine, Robert-R^ssle-Strasse 10, 13122 Berlin, Germany

**Brown, P. M., Tagari, P., Rowan, K. R., Yu, V. L., O'Neill, G. P., Middaugh, C. R., Sanyal, G., Ford-Hutchinson, A. W., Nicholson, D. W. Epitope-labeled soluble human interleukin-5 (IL-5) receptors. Affinity cross-link labeling, IL-5 binding, and biological activity. J. Biol. Chem. 270, 29236-29243 (1995)

Optima XL-A, sed. equil., m; recombinant-soluble IL-5 receptor domain and its interleukin-5 complex; An-60 Ti, 16 and 22 krpm, 4deg.C; BIAcore, CD and fluorescence also used; (Nicholson) Dept. of Biochemistry and Molecular Biology, Merck Frosst Centre for Therapeutic Research, P.O. Box 1005, Pointe Claire-Dorval, Quebec H9R 4P8, Canada

**Bubb, M. R., Knutson, J. R., Porter, D. K., Korn, E. D. Actobindin induces the acccumulation of actin dimers that neither nucleate polymerization nor self-associate. J. Biol. Chem. 269, 25592- 25597 (1994)

Optima XL-A, sed. vel., D, S; actobindin-actin interaction; An-60 Ti, 53 krpm, 4deg.C, 290 nm; fluorescence anisotropy also; (Korn) Lab. of Cell Biol., NHLBI, Natl. Institutes of Health, Bethesda, MD 20892

**Dong, F., Gogol, E. P., von Hippel, P. H. The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon activation by nucleoside triphosphate. J. Biol. Chem. 270, 7462-7473 (1995)

Optima XL-A, sed. vel., S; bacteriophage T4 helicase and its GTP-gamma-S or NTP complexes; An-D or An-F, 50 krpm, 280 nm, SEC & electron microscopy also; state of association; (von Hippel) Institute of Molecular Biology and Dept. of Chemistry, Univ. of Oregon, Eugene, OR 97403-1229

**Fiebrig, I., Harding, S. E., Davis, S. S. Sedimentation analysis of potential interactions between mucins and a putative bioadhesive polymer. Progress in Colloid & Polymer Science, Vol. 94, pp. 66-73. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. vel., S; pig gastric mucin-chitosan complex; 2 & 10 krpm, 230 nm; also MSE Centriscan & LS; (Fiebrig) National Centre for Macromolecular Hydrodynamics, School of Agriculture, Sutton Bonington, Nottingham, England

**Fless, G. M., Snyder, M. L., Furbee, J. W., Jr., Garcia-Hedo, M.-T., Mora, R. Subunit composition of lipoprotein(a) protein. Biochemistry 33, 13492-13501 (1994)

Optima XL-A, sed. equil., b.d., M(r); human plasma LDL, lipoprotein(a), reduced and carboxymethylated of apolipoproteins(a) and -(b), and apoB-apo(a) complex; 3-10 krpm, density adjusted with NaBr; GuHCl; (Fless) Dept. of Medicine, Univ. of Chicago, 5841 S. Maryland Ave., Chicago, IL 60637

**Fless, G. M., Furbee, J., Jr., Snyder, M. L., Meredith, S. C. Ligand-induced conformational change of lipoprotein(a). Biochemistry 35, 2289-2298 (1996)

Optima XL-A, sed. equil. in NaBr, M(r), v-bar; sed. vel., D, f/f(0), K(d), R(s), S; human LDL, Lp(a), and Lp(a-)ñ6-aminohexanoic acid complexes; rhesus monkey Lp(a) and its 6-AHA complex; An-60 Ti; 40 krpm (s.v.), 3500 rpm (diff.), 220 or 280 nm; effect of concentration; PAGE also used; Dept. of Medicine, Univ. of Chicago, 5841 S. Maryland Ave., Chicago, IL 60637

**Ghirlando, R., Keown, M. B., Mackay, G. A., Lewis, M. S., Unkeless, J. C., Gould, H. J. Stoichiometry and thermodynamics of the interaction between the Fc fragment of human IgG(1) and its low-affinity receptor Fc(gamma)RIII. Biochemistry 34, 13320-13327 (1995)

Optima XL-A, sed. equil., K(a), M(b), delta C, delta G, delta H, delta S; human IgG(1) fragment-receptor fragment interaction; 16 krpm, 280 nm, effect of temperature 1-28deg.C; LMB-NIDDK, Bldg. 5., Room 210, 5 Center Dr. MSCO540, Bethesda, MD 20892-0540

**Gonzalez, L., Jr., Plecs, J. J., Alber, T. An engineered allosteric switch in leucine-zipper oligomerization. Nat. Struct. Biol. 3, 510-515 (1996)

Optima XL-A, sed. equil., M(r), state of oligomerization; coiled-coil leucine zipper peptides and ligand complexes; 50 krpm, 235 and 220 nm, 5deg.C and 25deg.C; effect of benzene; CD also used; (Alber) Dept. of Molecular and Cell Biology, 229 Stanley Hall, Univ. of California, Berkeley, CA 94720-3206

**Horan, T., Wen, J., Arakawa, T., Liu, N., Brankow, D., Hu, S., Ratzkin, B., Philo, J. S. Binding of neu differentiation factor with the extracellular domain of Her2 and Her3. J. Biol. Chem. 270, 24604-24608 (1995)

Optima XL-A, sed. equil., stoichiometry; new differentiation factor-extracellular domains of Her2 or Her3 interaction; 8 or 12 krpm, 230 or 280 nm; light scattering and PAGE also used; Amgen Inc., Amgen Center, Thousand Oaks, CA 91320

**Horan, T., Wen, J., Narhi, L., Parker, V., Garcia, A., Arakawa, T., Philo, J. Dimerization of the extracellular domain of granulocyte-colony stimulating factor receptor by ligand binding: a monovalent ligand induces 2:2 complexes. Biochemistry 35, 4886-4896 (1996)

Optima XL-A, sed. equil., K, state of association; recombinant granulocyte-colony stimulating factor receptor and its ligand complex; 5800, 7000 and 8000 rpm; 230 or 280 nm; CD and light scattering/SEC also used; (Arakawa) Amgen Inc., Thousand Oaks, CA 91320-1789

**Jacobsen, M. P., Winzor, D. J. Characterization of the interactions of NADH with the dimeric and tetrameric states of methaemoglobin. Biochim. Biophys. Acta 1246, 17-23 (1995)

Optima XL-A, sed. equil., K(A), K(C); binding of NADH to methemoglobin dimers and tetramers; 12-16 krpm, 20deg.C; Centre for Protein Structure, Function and Engineering, Dept. of Biochemistry, Univ. of Queensland, Brisbane, Qld. 4072, Australia

**Johanson, K., Appelbaum, E., Doyle, M., Hensley, P., Zhao, B., Abdel-Meguid, S. S., Young, P., Cook, R., Carr, S., Matico, R., Cusimano, D., Dul, E., Angelichio, M., Brooks, I., Winborne, E., McDonnell, P., Morton, T., Bennett, D., Sokoloski, T., McNulty, D., Rosenberg, M., Chaiken, I. Binding interactions of human interleukin 5 with its receptor alpha subunit. Large scale production, structural, and functional studies of Drosophila-expressed recombinant proteins. J. Biol. Chem. 270, 9459-9471 (1995)

Optima XL-A, sed. equil., m, stoichiometry; a recombinant human interleukin 5, its receptor alpha subunit and complex; 25deg.C; PAGE, size exclusion chromatrography, mass spectrometry, and filtration microcalorimetry also used; (Chaiken) Dept. of Molecular Immunology, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406

**Keown, M. B., Ghirlando, R., Young, R. J., Beavil, A. J., Owens, R. J., Perkins, S. J., Sutton, B. J., Gould, H. J. Hydrodynamic studies of a complex between the Fc fragment of human IgE and a soluble fragment of the Fc-epsilon-RI alpha chain. Proc. Natl. Acad. Sci. 92, 1841-1845 (1995) Optima XL-A, sed. equil., M(b); sed. vel., S; recombinant human IgE, its Fc-epsilon-RI receptor fragment, and complex; 11-17 krpm & 18-22 krpm (s.e.); 40 & 50 krpm (s.v.); 280 nm; PAGE also used; (Gould) The Randall Institute, King's College London, 26-29 Drury Lane, London WC2B 5RL, UK

**Kilby, P. M., Primrose, W. U., Roberts, G. C. K. Changes in the structure of bovine phospholipase A(2) upon micelle binding. Biochem. J. 305, 935-944 (1995)

Optima XL-A, sed. equil., m of protein component; beef pancreatic phospholipase A(2)-SDS complexes; 18 or 40 krpm, 280 nm, 20deg.C; effect of D(2)O; Dept. of Biochemistry and Biological NMR Centre, Univ. of Leicester, Adrian Building, University Road, Leicester, LE1 7RH, UK

**Kleinekofort, W., Germeroth, L., van den Broek, J. A., Schubert, D., Michel, H. The light-harvesting complex II (B800/850) from Rhodospirillum molischianum is an octamer. Biochim. Biophys. Acta 1140, 102-104 (1992)

Optima XL-A, sed. equil., M(r),v-bar; light-harvesting complexñdetergent complexes; 9-25 krpm, 373 and 494 nm; LDAO and C(12)E(8) detergents; Inst. Biophysik der JWG-Universitat and MPI fur Biophysik, Frankfurt am Main, Germany

**Kortt, A. A., Malby, R. L., Caldwell, J. B., Gruen, L. C., Ivancic, N., Lawrence, M. C., Howlett, G. J., Webster, R. G., Hudson, P. J., Colman, P. M. Recombinant anti-sialidase single-chain variable fragment antibody. Characterization, formation of dimer and higher-molecular-mass multimers and the solution of the crystal structure of the single-chain variable fragment/sialidase complex. Eur. J. Biochem. 221, 151-157 (1994)

Optima XL-A, sed. equil., m; complexes of tern sialidase with rec single-chain variable fragment antibody monomer and dimer; Airfuge sed. equil. for K(a) determination., SEC & GF also used; (Kortt) CSIRO, Division of Biomolecular Engineering, 343 Royal Parade, Parkville, Victoria 3052, Australia

**Laue, T. M., Senear, D. F., Eaton, S., Ross, J. B. A. 5-Hydroxytryptophan as a new intrinsic probe for investigating protein-DNA interactions by analytical ultracentrifugation. Study of the effect of DNA on self-assembly of the bacteriophage lambda cI repressor. Biochemistry 32, 2469-2472 (1993)

Optima XL-A, sed. equil., M(r) bacteriophage lambda cI repressor-oligonucleotide binding; 10 krpm; (Laue) Dept. of Biochemistry and Molecular Biology, Univ. of New Hampshire, Durham, NH 03824

**Linsdell, H., Toiron, C., Bruix, M., Rivas, G., Menendez, M. Dimerization of A82846B, vancomycin and ristocetin: influence on antibiotic complexation with cell wall model peptides. J. Antibiot. 49, 181-193, (1996)

Optima XL-A, sed. equil., K; glycopeptide antibiotics A82846B, vancomycin and ristocetin and their cell wall model peptide complexes; 40 krpm; 240, 280 and 300 nm; 25deg.C; NMR also used; Instituto "Rocasolano", Serrano 119, Spain

**Lobert, S., Vulevic, B., Correia, J. J. Interaction of vinca alkaloids with tubulin: a comparison of vinblastine, vincristine, and vinorelbine. Biochemistry 35, 6806-6814 (1996)

Optima XL-A, sed. vel., g(s), K; pig brain tubulin interaction with vinblastine, vincristine and vinorelbine; An-60 Ti, 30 or 42 krpm, 280 nm, 5, 25 or 36deg.C; self-association; stopped-flow light scattering and electron microscopy also used; School of Nursing, Univ. of Mississippi Medical Ctr., 2500 N. State St., Jackson, MS 39216

**Lu, M., Blacklow, S. C., Kim, P. S. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nature, Struct. Biol. 2, 1075-1082 (1995)

Optima XL-A, sed. equil., M(r), state of oligomerization; recombinant HIV-1 envelope peptide heterodimer complexes; 15 and 18 krpm, 20deg.C, effect of concentration; CD also used; (Kim) Howard Hughes Medical Inst., Whitehead Inst. for Biomedical Research, Dept. of Biology, Massachusetts Inst. of Technology, Cambridge, MA 02142

**Lewis, M. S., Shrager, R. I., Kim, S.-J. Analysis of protein-nucleic acid and protein-protein interactions using multi-wavelength scans from the XL-A analytical ultracentrifuge. Modern Analytical Ultracentrifugation, pp. 94-115. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Optima XL-A, sed. equil.; Drosophila heat shock factor-DNA binding; computer simulation of protein-protein interactions; multiple scans taken betwen 230 nm & 240 nm; BEIP, NCRR, National Institute of Health, Bethesda, MD 20892

**Lewis, M. S., Shrager, R., Kim, S. J. Ultracentrifugal analysis of protein-nucleic acid interactions using multi-wavelength scans. Progress in Colloid & Polymer Science, Vol. 94, pp. 46-53. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil., absorbancy distributions at multiple wavelengths; Drosophila heat shock factor polypeptide, synthetic oligodeoxynucleotide and their interaction; 230-246, 260 & 280 nm; (Lewis) Biomedical Engineering and Instrumentation Program, National Center for Research Resources, Bethesda, MD

**Lin, K., Hwang, P. K., Fletterick, R. J. Mechanism of regulation in yeast glycogen phosphorylase. J. Biol. Chem. 270, 26833-26839 (1995)

Optima XL-A, sed. equil., m, state of oligomerization; recombinant native and mutant glycogen phosphorylases and their activator or inhibitor complexes; 5000 rpm, 280 nm, 25deg.C; PAGE also used; (Fletterick) Dept. of Biochemistry and Biophysics, Univ. of California, San Francisco, CA 94143-0448

**Liu, J., Lester, P., Builder, S., Shire, S. J. Characterization of complex formation by humanized anti-IgE monoclonal antibody and monoclonal human IgE. Biochemistry 34, 10474-10482 (1995)

Optima XL-A, sed. equil., M(w); sed. vel., g(s)*, S; monoclonal IgE, humanized anti-IgE monoclonal antibody and their complexes; 5, 7 and 10 krpm (s.e.), 60 krpm (s.v.), 10deg.C; size exclusion chromatography also used; hydrodynamic models; (Shire) Pharmaceutical Research and Development and Recovery Process Research and Development, Genentech, Inc., South San Francisco, CA 94080

**Lobert, S., Frankfurter, A., Correia, J. J. Binding of vinblastine to phosphocellulose-purified and alpha/beta-class III tubulin: the role of nucleotides and beta-tubulin isotypes. Biochemistry 34, 8050-8060 (1995)

Optima XL-A, sed. vel., g(s), S; binding of vinblastine to tubulin; An-60 Ti, 30 or 42 krpm, 230-280 nm, 5, 24.6 or 35.5deg.C; effect of nucleotides; electron microscopy also used. (Lobert) School of Nursing, Univ. of Mississippi Med. Ctr., 2500 N. State St., Jackson, MS 39216

**Mach, H., Volkin, D. B., Burke, C. J., Middaugh, C. R., Linhardt, R. J., Fromm, J. R., Loganathan, D., Mattsson, L. Nature of the interaction of heparin with acidic fibroblast growth factor. Biochemistry 32, 5480-5489 (1993)

Optima XL-A, sed. equil., effect of various concentrations on m & stoichiometry; acidic fibroblast growth factor-heparin complexes; 5-30 krpm; also surface plasmon resonance & light scattering; (Mach) Dept. of Pharmaceutical Research, Merck Research Laboratories, WP26-331, West Point, PA 19486

**Malchiodi, E. L., Eisenstein, E., Fields, B. A., Ohlendorf, D. H., Schlievert, P. M., Karjalainen, K., Mariuzza, R. A. Superantigen binding to a T cell receptor beta chain of known three-dimensional structure. J. Exp. Med. 182, 1833-1845 (1995)

Optima XL-A, sed. equil., K(d), M; recombinant T-cell receptor beta-chain, bacterial toxin superantigens, and their complexes; An 55, 22-30 krpm, 20-25deg.C; BIAcore also used and K(d)s compared with XL-A data; (Mariuzza) Center for Advanced Research in Biotechnology, 9600 Gudelsky Dr., Rockville, MD 20850

**Mendoza, J. A., Horowitz, P. M. Bound substrate polypeptides can generally stabilize the tetradecameric structure of Cpn60 and induce its reassembly from monomers. J. Biol. Chem. 269, 25963-25965 (1994)

Optima XL-A, sed. vel., S; chaperonin Cpn60-polypeptide substrate complexes state of dissociation; An-60 Ti, 27 krpm; (Horowitz) Dept Biochem., Univ. of Texas Health Science Center, San Antonio, TX 78240-7760

**Mendoza, J. A., Demeler, B., Horowitz, P. M. Alteration of the quaternary structure of cpn60 modulates chaperonin-assisted folding. Implications for the mechanism of chaperonin action. J. Biol. Chem. 269, 2447-2451 (1994)

Optima XL-A, sed. equil. (m detd. but not reported); sed. vel., S; chaperonin 60 and its rhodanese complex in presence of urea; An-60-Ti, 4500 rpm, 27 krpm and 44 krpm; Gastrointestinal Research Laboratory (151M2), Dept. of Veterans Affairs Medical Center and Dept. of Medicine, Univ. of California, San Francisco, CA 94121

**Nagahora, H., Harata, K., Muraki, M., Jigami, Y. Site-directed mutagenesis and sugar-binding properties of the wheat germ agglutinin mutants Tyr73Phe and Phe116Tyr. Eur. J. Biochem. 233, 27-34 (1995)

Optima XL-A, sed. equil., K(a), m; wheat germ agglutinins and binding of N-acetylglucosamine; 16 krpm, 280 nm; (Jigami) Molecular Biology Dept., National Institute of Bioscience and Human Technology, 1-1 Higashi, Tsukuba, Ibaraki, Japan 305

**Olsen, P. H., Esmon, N. L., Esmon, C. T., Laue, T. M. Ca(2+) dependence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation. Biochemistry 31, 746-754 (1992)

Optima XL-A, sed. vel., f, S; protein C-thrombin-thrombomodulin complex; 60 krpm, 4-hole rotor, double-sector cells, 20-21deg.C; (Laue) Dept. of Biochemistry, Spaulding Life Sciences Building, Univ. of New Hampshire, Durham, NH 03824.

**Olson, M. W., Dallmann, H. G., McHenry, C. S. DnaX complex of Escherichia coli DNA polymerase III holoenzyme. The chi-psi complex functions by increasing the affinity of tau and gamma for delta*delta( to a physiologically relevant range. J. Biol. Chem. 270, 29570-29577 (1995)

Optima XL-A, sed. equil., M; sed. vel., D, S, Stokes' radius; bacterial DNA polymerase III chi-psi heterodimer complex; An-60 Ti, 15-35 krpm (s.e.), 40 krpm (s.v.), 230 and 280 nm, 4deg.C; BIAcore also used; (McHenry) Dept. of Biochemistry, Biophysics and Genetics and Graduate Program in Molecular Biology, Univ. of Colorado Health Sciences Center, Denver, CO 80262

**Pantoliano, M. W., Horlick, R. A., Springer, B. A., Van Dyk, D. E., Tobery, T., Wetmore, D. R., Lear, J. D., Nahapetian, A. T., Bradley, J. D., Sisk, W. P. Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization. Biochemistry 33, 10229-10248 (1994)

Optima XL-A, sed. equil., M(w); recombinant fibroblast growth factor receptor and its complexes with FGF and FGF-heparin; isothermal titrating calorimetry also used; (Pantoliano) 3-Dimensional Pharmaceuticals Inc., 3700 Market St., Philadelphia, PA 19104

**Pennica, D., Lam, V. T., Weber, R. F., Kohr, W. J., Basa, L. J., Spellman, M. W., Ashkenazi, A., Shire, S. J., Goeddel, D. V. Biochemical characterization of the extracellular domain of the 75-kilodalton tumor necrosis factor receptor. Biochemistry 32, 3131-3138 (1993)

Optima XL-A, sed. equil., M(r); recombinant human tissue factor-alpha, -beta, receptor, and complexes; 15 krpm, 235 nm; Depts. of Molecular Biology, Protein Chemistry, Medicinal and Analytical Chemistry, Pulmonary Research, and Pharmaceutical Research and Development, Genentech, Inc., 460 Point San Bruno Blvd., South San Francisco, CA 94080

**Philo, J., Talvenheimo, J., Wen, J., Rosenfeld, R., Welcher, A., Arakawa, T. Interactions of neurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3(BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors. J. Biol. Chem. 269, 27840-27846 (1994)

Optima XL-A, sed. equil., K(d); neurotrophins-receptors interactions; 10-14 krpm; Amgen Inc., Thousand Oaks, CA 91320-1789

**Philo, J. S., Aoki, K. H., Arakawa, T., Narhi, L. O., Wen, J. Dimerization of the extracellular domain of the erythropoietin (EPO) receptor by EPO: one high-affinity and one low-affinity interaction. Biochemistry 35, 1681-1691 (1996)

Optima XL-A, sed. equil., K(d), M(r); recombinant glycosylated and deglycosylated erythropoietin receptor-erythropoietin interaction; 10, 11, 15 and 18 krpm (also final run at 48 krpm to establish baseline); 230 and 280 nm; light scattering/size exclusion chromatography and titration calorimetry also used; Protein Chemistry Dept., Amgen, Inc., Amgen Ctr., Thousand Oaks, CA 91320

**Philo, J. S., Wen, J., Wypych, J., Schwartz, M. G., Mendiaz, E. A., Langley, K. E. Human stem cell factor dimer forms a complex with two molecules of the extracellular domain of its receptor, Kit. J. Biol. Chem. 271, 6895-6902 (1996)

Optima XL-A, sed. equil., K(d), state of association; recombinant stem cell factor-Kit receptor complex; 8, 11 and 14 krpm; 215, 230 and 280 nm; light scattering/SEC and titration calorimetry also used; (Langley) Amgen Inc., 1840 DeHavilland Dr., Thousand Oaks, CA 91320-1789

**Riley, L. G., Ralston, G. B., Weiss, A. S. Multimer formation as a consequence of separate homodimerization domains: the human c-Jun leucine zipper is a transplantable dimerization module. Protein Eng. 9, 223-230 (1996)

Optima XL-A and Model E with interference optics, sed. equil., M(w) (Da), state of association; c-Jun and c-Fos leucine zipper domain-glutathione transferase fusion proteins; 20 or 18 krpm, 280 and 360 nm, 20deg.C; PAGE and gel filtration also used; (Weiss) Dept. of Biochemistry, Univ. of Sydney, NSW 2006, Australia

**Rivas, G., Tangemann, K., Minton, A. P., Engal, J. Binding of fibrinogen to platelet integrin alpha-IIb-beta-3 in solution as monitored by tracer sedimentation equilibrium. J. Mol. Recognit. 9, 31-38 (1996)

Optima XL-A, tracer sed. equil., K(d); integrin alpha-IIb-beta-3ñfibrinogen binding; 3-10 krpm, 280-290 nm or 495-550 nm, 10deg.C; with and without detergent; electron microscopy also used; Centro de Investigaciones Biologicas, CSIC, Velazquez 144, 28006-Madrid, Spain

**Sackett, D. L. Vinca site agents induce structural changes in tubulin different from and antagonistic to changes induced by colchicine site agents. Biochemistry 34, 7010-7019 (1995)

Optima XL-A, sed. vel., state of association; interaction of vincristine and maytansine with tubulin; No exptl. details; state of association; fluorescence also used; Natl. Inst. of Health, Bldg. 8, Room 2A23, Bethesda, MD 20892

**Sackett, D. L., Kosk-Kosicka, D. The active species of plasma membrane Ca(2+)-ATPase are a dimer and a monomer-calmodulin complex. J. Biol. Chem. 271, 9987-9991 (1996)

Optima XL-A and Model E with Scanner, sed. equil., m, state of oligomerization; erythrocyte membrane Ca(2+)-ATPase dimer and monomer-calmodulin complex; An-60 Ti, 12-15 krpm; 230, 280 and 350 nm, 20 or 25deg.C; (Kosk-Kosicka) Dept. of Anesthesiology/Critical Care Medicine, The Johns Hopkins Univ. School of Medicine, Baltimore, MD 21287

**Saez, C. T., Jansen, G. J., Smith, A., Morgan, W. T. Interaction of histidineñproline-rich glycoprotein with plasminogen: effect of ligands, pH, ionic strength, and chemical modification. Biochemistry 34, 2496-2503 (1995)

Optima XL-A, sed. equil., K(d), M; FITC-plasminogen interaction with histidineñproline-rich glycoprotein; An-60 Ti, 10 krpm & 30-10 krpm, 495 nm; effect of temperature (25-4deg.C); sucrose gradient centrifugation (VTi 80) also used; (Morgan) Univ. of MissouriñKansas City, Division of Biochemistry and Molecular Biology, School of Biological Sciences, Kansas City, Missouri 64110

**Schuck, P. Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge. Progress in Colloid & Polymer Science, Vol. 94, pp. 1-13. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil., extinction profiles, M(r); human erythrocyte band 3 protein, DBDS nonionic detergent and oxyhemoglobin mixtures studied as model systems; 11-12,500 rpm; mathematical analysis described; 4deg.C, 270-340 nm; Institut fur Biophysik der Johann Wolfgang Goethe-Universitat and Max-Planck-Institut fur Biophysik, Frankfurt am Main, FRG

**Schuck, P., Legrum, B., Passow, H., Schubert, D. The influence of two anion-transport inhibitors, 4,4'-diisothiocyanatodihydrostilbene-2,2'-disulfonate and 4,4'-dibenzoylstilbene-2,2'-disulfonate, on the self-association of erythrocyte band 3 protein. Eur. J. Biochem. 230, 806-812 (1995)

Optima XL-A, sed. equil., state of association; human erythrocyte membrane band 3 protein and its interactions with stilbenedisulfonates; 9-12.5 krpm, 4deg.C, 280 nm; (Schubert) Institut fur Biophysik der J. W. Goethe-Univ. Theodor-Stern-Kai 7, Haus 74, D-60590 Frankfurt am Main, Germany

**Seifert, A., Heinevetter, L., C^lfen, H., Harding, S. E. Characterization of gliadin-galactomannan incubation mixtures by analytical ultracentrifugation. Part I. Sedimentation velocity. Carbohydr. Polym. 28, 325-332 (1995)

Optima XL-A, sed. equil., M(w); wheat gliadin and locust bean galactomannan; Model E and MOM 3170B analytical ultracentrifuge with schlieren optics, S; gliadin, galactomannan and their interaction; 10 and 15 krpm, 220 and 230 nm (XL-A); PAGE also used; German Institute for Human Nutrition, Arthur-Scheunert-Allee 114-116, D-14558 Bergholz-Rehbrucke, Germany

**Stafford, W. F., Liu, S., Prevelige, P. E. New high sensitivity sedimentation methods: application to the analysis of the assembly of bacteriophage P22. Techniques in Protein Chemistry, Vol. 6, pp. 427-434. Edited by J. W. Crabb. San Diego, Academic Press, 1995.

Optima XL-A with both absorption and video-based on-line interference optics, g(s*) vs. s*; bacteriophage P22 coat protein-bisANS dye interaction; Analytical Centrifugation Research Laboratory, Boston Biomedical Research Institute, Boston, MA 02114

**Ward, L. D., Howlett, G. J., Discolo, G., Yasukawa, K., Hammacher, A., Moritz, R. L., Simpson, R. J. High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor, and gp-130. J. Biol. Chem. 269, 23286-23289 (1994)

Optima XL-A, sed. equil., M; recombinant human interleukin-6, its receptor and IL-6-receptor-gp 130 complex; 12-, 10-, 8- and 6-krpm; BIAcore & SEC also used; (Simpson) Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Post Office Royal Melbourne Hospital, Parksville, Victoria 3050, Australia

**Ward, L. D., Hammacher, A., Howlett, G. J., Matthews, J. M., Fabri, L., Moritz, R. L., Nice, E. C., Weinstock, J., Simpson, R. J. Influence of interleukin-6 (IL-6) dimerization on formation of the high affinity hexameric IL-6:receptor complex. J. Biol. Chem. 271, 20138-20144 (1996)

Optima XL-A, sed. equil., M(r); recombinant human interleukin-6 monomer, dimer and their receptor complexes; 8 and 12 krpm, 20deg.C; BIAcore also used; (Simpson) Joint Protein Structure Laboratory, Ludwig Inst. for Cancer Research, P.O. Box 2008, Royal Melbourne Hospital, Victoria, 3050, Australia

**Wilson, T. J., Argaet, V. P., Howlett, G. J., Davidson, B. E. Evidence for two aromatic amino acid-binding sites, one ATP-dependent and the other ATP-independent, in the Escherichia coli regulatory protein TyrR. Mol. Microbiol. 17, 483-492 (1995)

Optima XL-A, sed. equil., K(a), K(d); bacterial regulatory protein TyrR-amino acid ligand binding; An-60 Ti, 8 krpm, 20deg.C, 285 and 293 nm; UV difference spectroscopy also used; (Davidson) Dept. of Biochemistry and Molecular Biology, The Univ. of Melbourne, Parkville, Victoria 3052, Australia

**Wu, M.-L., Morgan, W. T. Thermodynamics of heme-induced conformational changes in hemopexin: role of domain-domain interactions. Protein Sci. 4, 29-34 (1995)

Optima XL-A, sed. equil., K(d); rabbit serum hemopexin domain I-domain II interaction; 15 krpm; 280, 404 or 497 nm; titration calorimetry also used; Division of Molecular Biology and Biochemistry, School of Biological Sciences, Univ. of Missouri-Kansas City, Kansas City, MO 64110

**Wu, Z., Johnson, K. W., Goldstein, B., Choi, Y., Eaton, S. F., Laue, T. M., Ciardelli, T. L. Solution assembly of a soluble, heteromeric, high affinity interleukin-2 receptor complex. J. Biol. Chem. 270, 16039-16044 (1995)

Optima XL-A, interference optics, sed. equil., M(z); sed. vel., g(s*), interleukin-2 receptorñcoiled-coil complexes; 50 krpm; PAGE also; (Wu) Dept. of Pharmacology and Toxicology, Dartmouth Medical School, Hanover, NH 03755

**Yang, Y. R., Schachman, H. K. A bifunctional fusion protein containing the maltose-binding polypeptide and the catalytic chain of aspartate transcarbamoylase: assembly, oligomers, and domains. Biophys. Chem. 59, 289-297 (1996)

Optima XL-A, sed. equil., m, sed. vel., g*(s), S; recombinant maltose-binding protein complex and cleavage products; 50 krpm (s.v.), 235 or 280 nm, 20deg.C; PAGE also used; (Schachman) Dept. of Molecular and Cell Biology, Wendell M. Stanley Hall, Univ. of California, Berkeley, CA 94720-3206

**Yoo, S. H., Lewis, M. S. Thermodynamic study of the pH-dependent interaction of chromogranin A with an intraluminal loop peptide of the inositol 1,4,5-trisphosphate receptor. Biochemistry 34, 632-638 (1995)

Optima XL-A, sed. equil., delta C, delta G, delta H, delta S; chromagranin A-intraluminal loop peptide interaction; 10 krpm; 6, 10, 14, 18 & 22deg.C; 280, 290, 295, 300, 305 & 310 nm; multiwavelength scans; effect of pH, temperature & calcium ion; Laboratory of Cellular Biology, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, MD 20892

**Yoo, S. H., Lewis, M. S. Effects of pH and Ca(2+) on heterodimer and heterotetramer formation by chromogranin A and chromogranin B. J. Biol. Chem. 271, 17041-17046 (1996)

Optima XL-A, sed. equil., delta C, delta G, delta H, T delta S; beef adrenal chromogranin A and chromogranin B heterodimer and heterotetramer formation; 8 krpm, 2, 5, 8, 11, 14, 17, and 20deg.C; 280 nm, effect of pH and temperature; Laboratory of Neurochemistry, 5 Research Court, 2A37 NIDCD, Natl. Inst. of Health, Bethesda, MD 20892-3320

General Studies

**Adams, E. T., Jr. Sedimentation coefficients of self-associating species. Analysis of monomer-dimer-n-mer associations and some indefinite associations. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 407-427. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation velocity analysis theory for self-associating systems; Chemistry Dept., Texas A & M Univ., College Station, TX 77843

**Ansevin, A. T., Roark, D. E., Yphantis, D. A. Improved ultracentrifuge cells for high-speed sedimentation equilibrium studies with interference optics. Anal. Biochem. 34, 237-261 (1970)

**Arakawa, T., Timasheff, S. N. Calculation of the partial specific volume of proteins in concentrated salt and amino acid solutions. Methods in Enzymology, Vol. 117, pp. 60-65. Edited by C. H. W. Hirs and S. N. Timasheff. New York, Academic Press, 1985.

**Attri, A. K., Lewis, M. S. A fitting function for the analysis of sedimentation velocity concentration distributions. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 138-146. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Model E with absorption optics, sed. vel. concentration distributions for ovalbumin, rabbit muscle aldolase-bovine serum albumin mixture; Lab. of Cell Biology, National Heart, Lung and Blood Institute and Biomedical Engineering and Instrumentation Program, National Center for Research Resources, National Institutes of Health, Bethesda, MD 20892

**Baldwin, R. L. Boundary spreading in sedimentation velocity experiments. III. Effects of diffusion on the measurement of heterogeneity when concentration dependence is absent. J. Phys. Chem. 58, 1081-1086 (1954)

**Becerra, S. P., Kumar, A., Lewis, M. S., Widen, S. G., Abbotts, J., Karawya, E. M., Hughes, S. H., Shiloach, J., Wilson, S. H. Protein-protein interactions of HIV-1 reverse transcriptase: implication of central and C-terminal regions in subunit binding. Appendix: Ultracentrifugal analysis of mixed association, by M. S. Lewis. Biochemistry 30, 11707-11719 (1991)

Data analysis for heteroassociation

**Beckett, D., Nenortas, E. Measurement of protein-protein association equilibria by large zone analytical gel filtration chromatography and equilibrium analytical ultracentrifugation. Adv. Biophys. Chem. 5, 233-262 (1995)

The Optima XL-A and Model E are both mentioned in this overview

**Borchard, W. Swelling pressure equilibrium of swollen crosslinked systems in an external field. I. Theory. Progress in Colloid & Polymer Science, Vol. 86, pp. 84-91. Edited by H.-G. Kilian, G. Lagaly and W. Borchard. Darmstadt, Steinkopff Verlag, 1991.

Theory of gel behavior of crosslinked substances in an ultracentrifugal field; Angewandte Physikalische Chemie der Universitat GH Duisburg, FRG

**Borchard, W. The sedimentation diffusion equilibrium of a ternary gel. Progress in Colloid & Polymer Science, Vol. 94, pp. 82-89. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Sedimentation equilibrium theory for ternary gels; Angewandte Physikalische Chemie der Universitat GH Duisburg, FRG

**Braswell, E. H. Polyelectrolyte charge corrected molecular weight and effective charge by sedimentation. Biophys. J. 51, 273-281 (1987)

Unspecified analytical ultracentrifuge, interference optics, sed. equil., sed. vel., calculation of effective charge and true molecular weight of polyelectrolytes

**Budd, P. M. Sedimentation analysis of synthetic polyelectrolytes. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 593-608. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation velocity and sedimentation equilibrium theory; concentration dependence of s; frictional coefficient; Dept. of Chemistry, Univ. of Manchester, Oxford Road, Manchester, M13 9PL U.K.

**Budd, P. M. Sedimentation and diffusion of polyelectrolytes. Progress in Colloid & Polymer Science, Vol. 94, pp. 107-115. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Sedimentation velocity and diffusion behavior of polyelectrolytes; Dept. of Chemistry, Univ. of Manchester, Manchester, UK

**Cann, J. R. Theory of sedimentation for ligand-mediated heterogeneous association-dissociation reactions. Biophys. Chem. 16, 41-49 (1982)

**Cann, J. R. Computer simulation of the sedimentation of ligand-mediated and kinetically controlled macromolecular interactions. Modern Analytical Ultracentrifugation, pp. 171-188. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Dept. of Biochemistry/Biophysics/Genetics, Univ. of Colorado, Denver, CO 80262

**Cann, J. R., Coombs, R. O., Howlett, G. J., Jacobsen, M. P., Winzor, D. J. Effects of molecular crowding on protein self-association: a potential source of error in sedimentation coefficients obtained by zonal ultracentrifugation in a sucrose gradient. Biochemistry 33, 10185-10190 (1994)

Optima XL-A, sed. vel., S; results compared with simulated run in SW 60 Ti with a sucrose gradient; yeast enolase used as a model dimerizing system; 60 krpm; effect of sucrose on polymerization equilibrium; (Winzor) Dept. of Biochemistry, Univ. of Queensland, Brisbane, QLD4072, Australia

**Chatelier, R. C., Minton, A. P. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. I. Self-associating proteins. Biopolymers 26, 507-524 (1987)

Simulation of sedimentation equilibrium of self-associating systems; estimation of true weight-average molecular weight; Dept. of Biochemistry/Biophysics/Genetics, Univ. of Colorado, Denver, CO 80262

**Chatelier, R. C., Minton, A. P. Sedimentation equilibrium in macromolecular solutions of arbitrary concentration. II. Two protein components. Biopolymers 26, 1097-1113 (1987)

Simulation of sedimentation equilibrium of heteroassociations; estimation of true weight-average molecular weight

**C^lfen, H. Analytical ultracentrifugation of gels. Colloid Polym. Sci. 273, 1101-1137 (1995)

A review of analytical ultracentrifugation studies of both biological and synthetic gels; Max-Planck-Institute for Colloid and Interface Research, Colloid Chemistry Dept., Kanstrasse 55, 14513 Taltow-Seehof, Germany

**C^lfen, H., Holtus, G., Borchard, W. Multifunctional cell for measurements of temperature, distance, and refractive index as for determining optical calibration factors in rotating systems. Rev. Sci. Instr. 64, 2999-3005 (1993)

Special temperature-measuring cell that can be used in Model E or XL-A; Angewandte Physikalische Chemie der Univ.-GH-Duisburg, Lotharstr. 1, D47048 Duisburg, Germany

**C^lfen, H., Harding, S. E.. A study on Schlieren patterns derived with the Beckman Optima XL-A UV-absorption optics. Progress in Colloid & Polymer Science, Vol. 99, pp. 167-186. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A, sed. vel., schlieren effect derived with absorption optics used to examine various polysaccharides: chitosan, kappa-carrageenan, Na-alginate, dextrans 20 and 150, and xanthan; 12.6-60 krpm, 20deg.C, 276-600 nm; results compared to Model E with schlieren optics; Max-Planck-Inst. for Colloid and Interface Research, Colloid Chemistry Dept., Kantstrasse 55, 14513 Teltow, Germany

**Condino, J. The determination of molecular weights by sedimentation equilibrium. Technical Information DS-820. Palo Alto, Calif., Spinco Business Unit, 1992.

Brief overview of sedimentation equilibrium

**Condino, J. Sample preparation for analytical ultracentrifugation in the Optimaô XL-A. Technical Information LXL/A-AN-001. Palo Alto, Calif., Spinco Business Unit, 1992.

**Correia, J. J., Yphantis, D. A. Equilibrium sedimentation in short solution columns. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 231-252. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Model E, interference optics, short-column sedimentation equilibrium methodology; Dept. of Molecular and Cell Biology, Univ. of Connecticut, Box U-125, Storrs, CT 06269-3125

**Cox, D. J., Dale, R. S. Simulation of transport experiments for interacting systems. Protein-Protein Interactions, pp. 173-211. Edited by C. Frieden and L. W. Nichol. New York, John Wiley & Sons, 1981.

**Creeth, J. M., Knight, C. G. On the estimation of the shape of macromolecules from sedimentation and viscosity measurements. Biochim. Biophys. Acta 102, 549-558 (1965)

**Darawshe, S., Minton, A. P. Quantitative characterization of macromolecular associations in solution via real-time and postcentrifugation measurements of sedimentation equilibrium: a comparison. Anal. Biochem. 220, 1-4 (1994)

Optima XL-A and Brandel FR-115 Microfractionator techniques are compared and deemed complementary; Laboratory of Biochemical Pharmacology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892

**de la Torre, J. G. Sedimentation coefficients of complex biological particles. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 333-345. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation velocity theory for rigid, spherical particles, ellipsoids, cylinders, bead models; table of sedimentation, diffusion & frictional ratios for monomers to octamers of different shapes; Dept. de Quimica Fisica, Facultad de Ciencias Quimicas y Matematicas Univ. de Murcia, 30071 Murcia, Spain

**Dhami, R., C^lfen, H., Harding, S. E. A comparative "Schlieren" study of the sedimentation behaviour of three polysaccharides using the Beckman Optima XL-A and Model E analytical ultracentrifuges. Progress in Colloid & Polymer Science, Vol. 99, pp. 187-192. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A schlieren effect results compared with Model E schlieren results, sed. vel., K(s), S; polysaccharides: arabinoxylan, xanthan and locust bean gum; 30 or 60 krpm, 200-600 nm, 20deg.C; (Harding) Natl. Ctr. for Macromolecular Hydrodynamics, Univ. of Nottingham, Sutton Bonington Campus, Loughborough LE12 5RD, UK

**Durchschlag, H., Zipper, P. Calculation of the partial volume of organic compounds and polymers. Progress in Colloid & Polymer Science, Vol. 94, pp. 20-39. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Tables of partial molar volume increments for selected atoms and atomic groups; table of calculated and experimental partial specific volumes of organic compounds and biochemicals; (Durchschlag) Institute of Biophysics and Physical Biochemistry, Univ. of Regensburg, FRG

**Ebel, C. Characterisation of the solution structure of halophilic proteins. Analytical centrifugation among complementary techniques (light, neutron and X-ray scattering, density measurements). Progress in Colloid & Polymer Science, Vol. 99, pp. 17-23. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Overview of complementary techniques used for studies of halophilic proteins; Institut de Biologie Structurale, 41 Avenue des Martyrs, 38 027 Grenoble Cedex 1, France

**Edelstein, S. J., Schachman, H. K. The simultaneous determination of partial specific volumes and molecular weights with microgram quantities. J. Biol. Chem. 242, 306-311 (1967)

**Edsall, J. T. Apparent molal volume, heat capacity, compressibility and surface tension of dipolar ions in solutions. Proteins, Amino Acids and Peptides as Ions and Dipolar Ions, pp. 155-176. Edited by E. J. Cohn, and J. T. Edsall. New York, Rheinhold, 1943.

**Eisenberg, H. Protein and nucleic acid hydration and cosolvent interactions: establishment of reliable baseline values at high cosolvent concentrations. Biophys. Chem. 53, 57-68 (1994)

Optima XL-A mentioned in this overview of methods including light, neutron, and X-ray scattering; Dept. of Structural Biology, Weizmann Inst. of Science, Rehovot 76100, Israel

**Eisenberg, H. Birth of the macromolecule. Biophys. Chem. 59, 247-257 (1996)

Historical overview of early macromolecular chemistry and the Svedberg's analytical ultracentrifuge; Dept. of Structural Biology, Weizmann Institute of Science, Rehovot 76100, Israel

**Freire, J. J., de la Torre, J. G. Sedimentation coefficients of flexible chain polymers. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 346-358. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation velocity theory; excluded volume & theta conditions; linear and nonlinear chains, branched chains, rings; (de la Torre) Dept. de Quimica Fisica, Facultad de Ciencias Quimicas y Matematicas Univ. de Murcia, 30071 Murcia, Spain

**Fujita, H. Notes on the derivation of sedimentation equilibrium equations. Modern Analytical Ultracentrifugation, pp. 3-14. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Sedimentation equilibrium theory; 35 Shimotakedono-Cho, Shichiku, Kita-Ku, Kyoto, Japan

**Furst, A. Overview of sedimentation velocity for the Optima XL-A Analytical Ultracentrifuge. Technical Information DS-819. Palo Alto, Calif., Spinco Business Unit, 1991.

Brief description of Optima XL-A; sedimentation velocity overview

**Genetic Engineering News. AU gains followers. Genet. Eng. News 13:4, 9, 29 (Feb. 15, 1993)

Comments of Optima XL-A users John Philo (Amgen), Preston Hensley (SmithKline Beecham), and Leo Einck (Hem Pharmaceuticals); Complementary techniques such as light scattering and mass spectroscopy also mentioned

**Giebeler, R. The Optima XL-A: a new analytical ultracentrifuge with a novel precision absorption optical system. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 16-25. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Description of the Optima XL-A hardware and data acquisition software

**Gmachowski, L. A universal curve representing the concentration and molecular weight dependences of sedimentation coefficient. Polym. J. 22, 771-775 (1990)

**Goldberg, R. J. Sedimentation in the ultracentrifuge. J. Phys. Chem. 57, 194-202 (1953)

**Gosting, L. J. Solution of boundary spreading equations for electrophoresis and the velocity ultracentrifuge. J. Am. Chem. Soc. 74, 1548-1552 (1952)

**Hansen, J. C., Lebowitz, J., Demeler, B. Analytical ultracentrifugation of complex macromolecular systems. Biochemistry 33, 13155-13163 (1994)

Overview of recent analytical ultracentrifuge studies, data acquisition and analysis, and future prospects of the Optima XL-A; Dept. Biochem., Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78284-7760

**Harding, S. E. Automatic data capture and analysis of Rayleigh interference fringe displacements in analytical ultracentrifugation. Opt. Lasers Eng. 8, 83-96 (1988)

**Harding, S. E. Analytical ultracentrifugation and the genetic engineering of macromolecules. Biotechnol. Genet. Eng. Rev. 11, 317-356 (1993)

Overview of analytical ultracentrifuge methods and applications; table of techniques for macromolecular physical characterization; review of genetically engineered products that have been characterized; National Centre for Macromolecular Hydrodynamics, School of Agriculture, Univ. of Nottingham, Sutton Bonington, UK

**Harding, S. E. Determination of macromolecular homogeneity, shape, and interactions using sedimentation velocity analytical ultracentrifugation. Microscopy, Optical Spectroscopy, and Macroscopic Techniques, pp. 61-73. Edited by C. Jones, B. Mulley, A. H. Thomas. Totowa, NJ, Humana Press, 1994.

The Optima XL-A is mentioned, along with other commercial ultracentrifuge models, in this brief overview of sedimentation velocity; Dept. of Applied Biochemistry and Food Science, Univ. of Nottingham, UK

**Harding, S. E. Determination of absolute molecular weights using sedimentation equilibrium analytical ultracentrifugation. Microscopy, Optical Spectroscopy, and Macroscopic Techniques, pp. 75-84. Edited by C. Jones, B. Mulley, A. H. Thomas. Totowa, NJ, Humana Press, 1994.

A brief overview of sedimentation equilibrium; Dept. of Applied Biochemistry and Food Science, Univ. of Nottingham, UK

**Harding, S. E. Sedimentation equilibrium analysis of glycopolymers. Progress in Colloid & Polymer Science, Vol. 94, pp. 54-65. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Overview of sedimentation equilibrium methods for determining molar mass of glycoconjugates and polysaccharides using schlieren or interference optics; Univ. of Nottingham, School of Agriculture, Sutton Bonington, UK

**Harding, S. E. The analytical ultracentrifuge spins again. Trends Anal. Chem. 13, 439-446 (1994)

Optima XL-A and Model E mentioned; overview of methodologies and their applications; National Centre for Macromolecular Hydrodynamics, Univ. of Nottingham School of Agriculture, Sutton Bonington, LE12 5RD, UK

**Harding, S. E. The sedimentation equilibrium analysis of polysaccharides and mucins: a guided tour of problem solving for difficult heterogeneous systems. Modern Analytical Ultracentrifugation, pp. 313-341. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Sedimentation equilibrium methods, nonideality factors, and data analysis for mucopolysaccharides; Univ. of Nottingham, School of Agriculture, Sutton Bonington LE12 5RD, UK

**Harding, S. E. On the hydrodynamic analysis of macromolecular conformation. Biophys. Chem. 55, 69-93 (1995)

Univ. of Nottingham, School of Agriculture, Sutton Bonington LE12 5RD, UK

**Harding, S. E. Some recent developments in the size and shape analysis of industrial polysaccharides in solution using sedimentation analysis in the analytical ultracentrifuge. Carbohydr. Polym. 28, 227-237 (1995)

Overview of sedimentation equilibrium and velocity methods, and review of applications; Optima XL-I mentioned; Univ. of Nottingham, Dept. of Applied Biochemistry and Food Science, Sutton Bonington LE12 5RD, UK

**Harding, S. E. Ultracentrifugation of food biopolymers. New Physico-Chemical Techniques for the Characterization of Complex Food Systems, pp. 109-138. Edited by E. Dickinson. London, Blackie Academic & Professional, 1995.

Optima XL-A, Model E and MOM analytical ultracentrifuges mentioned in this overview of techniques and applications to food biopolymers; tables listing sedimentation velocity parameters and shape characteristics of various food proteins, glycoproteins and polysaccharides; Dept. of Applied Biochemistry and Food Science, Univ. of Nottingham, UK

**Harding. S. E., C^lfen, H. Inversion formulae for ellipsoid of revolution macromolecular shape functions. Anal. Biochem. 228, 131-142 (1995)

(C^lfen) Colloid Chemistry Dept., Max-Planck Inst. for Colloid Research, D-14513 Teltow, Germany

**Harding, S. E., Rowe, A. J., Horton, J. C., eds. Analytical Ultracentrifugation in Biochemistry and Polymer Science. Cambridge, Royal Society of Chemistry, 1992.

Comprised of 33 papers mentioning use of both the Optima XL-A and Model E

**Harding, S. E., Horton, J. C., Morgan, P. J. MSTAR: a FORTRAN program for the model independent molecular weight analysis of macromolecules using low speed or high speed sedimentation equilibrium. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 275-294. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society

of Chemistry, 1992.

Optima XL-A, sed. equil., human IgM(1), MSTARA for data analysis; Univ. of Nottingham, Dept. of Applied Biochemistry and Food Science, Sutton Bonington, LE12 5rd U.K.

**Harrington, W. F. The effects of pressure in ultracentrifugation of interacting systems. Fractions 1975, No. 1, 10-18. (Fractions was formerly published by Beckman Instruments, Inc., Spinco Division, Palo Alto.)

**Harrington, W. F., Kegeles, G. Pressure effects in ultracentrifugation of interacting systems. Methods in Enzymology, Vol. 27, pp. 306-345. Edited by C. H. W. Hirs and S. N. Timasheff. New York, Academic Press, 1973.

**Hayes, D. B., Laue, T. M. A graphical method for determining the ideality of a sedimenting boundary. Modern Analytical Ultracentrifugation, pp. 245-258. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Model E, interference optics, sed. vel., graphical method for testing quality of sedimenting boundary using bovine serum albumin monomer as an example; Dept. of Biochemistry, Univ. of New Hampshire, Durham, NH 03824

**Hedges, J., Sarrafzadeh, S., Lear, J. D., McRorie, D. K. Extensions to commercial graphics packages for customization of analysis of analytical ultracentrifuge data. Modern Analytical Ultracentrifugation, pp. 227-244. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Optima XL-A data analysis using extended Originô (MicroCal Software, Inc.) software; examples of sedimentation equilibrium data analysis of coiled-coil Trp peptide given; Beckman Instruments, Inc., 1050 Page Mill Road, Palo Alto, CA 94304

**Hensley, P. Defining the structure and stability of macromolecular assemblies in solution: the re-emergence of analytical ultracentrifugation as a practical tool. Structure (London) 4, 367-373 (1996)

Overview of analytical ultracentrifuge methods and other techniques for characterizing molecular interactions; Optima XL-I mentioned; Figure 1 compares methods for interaction studies: mass spectrometry, surface plasmon resonance, AUC, calorimetry, and spectroscopy methods; Dept. of Macromolecular Sciences, SmithKline Beecham Pharmaceuticals, King of Prussia, PA 19406-0939

**Holzman, T. F., Snyder, S. W. Applications of analytical ultracentrifugation in structure-based drug design. Modern Analytical Ultracentrifugation, pp. 298-314. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Discussion of data acquisition and analysis methods for the Model E with Scanner, Prep UV Scanner and Optima XL-A; example analyses shown for ligand-induced association of CMP-KDO synthetase in D(2)O and human beta-amyloid A4 peptide; Abbott Laboratories, Protein Biochemistry, D-46Y Discovery Research, Pharmaceutical Products, Abbott Park, IL 60048.

**Horbett, T. A., Teller, D. C. An experimental study of baseline reproducibility and its effect on high-speed sedimentation equilibrium data. Anal. Biochem. 45, 86-99 (1972)

**Howlett, G. J. Sedimentation analysis of membrane proteins. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 470-483. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Discussion of both analytical and preparative ultracentrifuge methods, using sedimentation velocity, sedimentation equilibrium and density gradient techniques; determination of M, v-bar; Russell Grimwade School of Biochemistry, Univ. of Melbourne, Parkville 3052, Victoria, Australia

**Howlett, G. J., Jeffrey, P. D., Nichol, L. W. The effects of pressure on the sedimentation equilibrium of chemically reacting systems. J. Phys. Chem. 74, 3607-3610 (1970)

**Hsu, C. S., Minton, A. P. A strategy for efficient characterization of macromolecular heteroassociations via measurement of sedimentation equilibrium. J. Mol. Recognit. 4, 93-104 (1991)

Method for selecting experimental conditions for sedimentation equilibrium analysis of heteroassociating systems

**Huber, E., Schuck, P., Schubert, D. Analytische Ultrazentrifugation in der modernen Biochemie. LaborPraxis 2000, 55-56, 59-60 (1992)

Optima XL-A described; Institut fur Biophysik der Johann Wolfgang Goethe-Universitat, Theodor-Stern-Kai 7, Haus 74, 6000 Frankfurt/Main 70.

**Jacobsen, M. P., Winzor, D. J. Refinement of the omega analysis for the characterization of solute self-association by sedimentation equilibrium. Biophys. Chem. 45, 119-132 (1992)

Sedimentation equilibrium data analysis

**Jeffrey, P. Measuring protein molecular weights by equilibrium sedimentationóis the partial specific volume a problem? Today's Life Sci. 3:12, 50 (Dec. 1991)

Discussion of v-bar as a source of error in analytical ultracentrifugation; recommends use of 0.72 mL/g if amino acid composition is unknown

**Johnson, J. B., Becker, K., Edwards, G. Pressure corrections for CoCl(2) as a thermometer in an analytic ultracentrifuge. Anal. Biochem. 227, 385-387 (1995)

Pressure corrections given for 0-40deg.C; Dept. of Chemistry, Biochemistry, and Physics, Arkansas State Univ., State Univ., AR 72467

**Johnston, J. P., Ogston, A. G. A boundary anomaly found in the ultracentrifugal sedimentation of mixtures. Trans. Faraday Soc. 42, 789-799 (1946)

**Johnson, M. L., Straume, M. Comments on the analysis of sedimentation equilibrium experiments. Modern Analytical Ultracentrifugation, pp. 37-65. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Sedimentation equilibrium theory; Dept. of Pharmacology and Internal Medicine, Box 448, Univ. of Virginia Health Sciences Center, Charlottesville, VA 22908

**Joss, L. A., Ralston, G. B. beta-Lactoglobulin B: a proposed standard for the study of reversible self-association reactions in the analytical ultracentrifuge? Anal. Biochem. 236, 20-26 (1996)

Optima XL-A, sed. equil., delta G, delta H, delta S, state of association; beef milk beta-lactoglobulin B monomer-dimer; 25-30 krpm, 280 nm, 5-30deg.C; Dept. of Biochemistry, Univ. of Sydney, Sydney, New South Wales 2006, Australia

**Kegeles, G. Convection induced by hydrostatic pressure in sedimentation velocity experiments. Biopolymers 7, 83-86 (1969)

**Kegeles, G., Rhodes, L., Bethune, J. L. Sedimentation behavior of chemically reacting systems. Proc. Natl. Acad. Sci. 58, 45-51 (1967)

**Kegeles, G., Kaplan, S., Rhodes, L. The effects of pressure in high-speed ultracentrifugation of chemically reacting systems. Ann. N. Y. Acad. Sci. 164, 183-191 (1969)

**Kuntz, I. D. Hydration of macromolecules. III. Hydration of polypeptides. J. Am. Chem. Soc. 93, 514-516 (1971)

**Laue, T. M. On-line data acquisition and analysis from the Rayleigh interferometer. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 63-89. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Justification for interferometry vs. absorbance; solid state camera detectors; alignment; fringe displacement measurement; Dept. of Biochemistry, Univ. of New Hampshire, Durham, NH 03824

**Laue, T. M. Short column sedimentation equilibrium analysis for rapid characterization of macromolecules in solution. Technical Information DS-835. Palo Alto, Calif., Spinco Business Unit, 1992.

Short-column sedimentation equilibrium methods and applications

**Laue, T. M. Sedimentation equilibrium as thermodynamic tool. Methods in Enzymology, Vol. 259, pp. 427-452. Edited by M. L. Johnson and G. K. Ackers. San Diego, Academic Press, 1995.

Optima XL-A, sedimentation equilibrium protocol and extraction of thermodynamic quantities from data; Dept. of Biochemistry and Molecular Biology, Univ. of New Hampshire, Durham, NH 03824

**Laue, T. M. Analytical ultracentrifugation. Current Protocols in Protein Science, pp. 7.5.1-7.5.9. Edited by J. E. Coligan and others. N.Y., J. Wiley, 1996.

Introductory overview of analytical ultracentrifugation, including summaries of methods and alternative techniques, methods of solute detection, experimental design and troubleshooting guide; Univ. of New Hampshire, Durham, NH

**Laue, T. M., Rhodes, D. G. Determination of size, molecular weight, and presence of subunits. Methods in Enzymology, Vol. 182, pp. 566-587. Edited by M. P. Deutscher. San Diego, Academic Press, 1990.

Overview of various methods, including analytical ultracentrifugation

**Laue, T. M., Shah, B. D., Ridgeway, T. M., Pelletier, S. L. Computer-aided interpretation of analytical sedimentation data for proteins. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 90-125. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Discussion of data required for analysis; tables of v-bar for amino acids, carbohydrates, denaturants, detergents, ions, organic acids, glycerol, ethanol, etc.; solvent density; effect of buffer composition on rho; coefficients for power series for density and viscosity; estimating protein hydration and assymetry; axial ratio; Dept. of Biochemistry, Spaulding Life Sciences Building, Univ. of New Hampshire, Durham, NH 03824

**Laue, T. M., Anderson, A. L., Demaine, P. D. An on-line interferometer for the XL-A ultracentrifuge. Progress in Colloid & Polymer Science, Vol. 94, pp. 74-81. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Overview of design and use of a Rayleigh interference optical system for the Optima XL-A; Univ. of New Hampshire, Dept. of Biochemistry and Molecular Biology, Durham, NH

**Lavrenko, P. N. Analysis of polymer heterogeneity by sedimentation transport: 1. Method of moments, a new approach. Polymer 35, 2133-2136 (1994)

Method of moments procedure for determining polydispersity indices, such as M(z)/M(w), from sedimentation velocity data; Institute of Macromolecular Compounds, Russian Academy of Sciences, St. Petersburg 199004, Russia

**Lechner, M. D., Machtle, W. A new procedure for the determination of the molar mass distribution of polymers in solution from sedimentation equilibrium. Progress in Colloid & Polymer Science, Vol. 86, pp. 62-69. Edited by H.-G. Kilian, G. Lagaly and W. Borchard. Darmstadt, Steinkopff Verlag, 1991.

Unspecified analytical ultracentrifuge, interference or schlieren optics, molar mass distribution; polystyrenes, sodium polystyrene sulfonate

**Lechner, M. D., Machtle, W. A new procedure for the determination of molar mass distribution from sedimentation equilibrium runs in an analytical ultracentrifuge (AUC), 1. Measurements with interference optics. Makromol. Chem. 192, 1183-1192 (1991)

Model E, interference optics, sed. equil., M; polystyrene (Simplex procedure used to calculate number-, weight-, and z-average molecular weight); 4 & 5.6 krpm; 25 & 35deg.C

**Lee, J. C., Rajendran, S. Studies of macromolecular interaction by sedimentation velocity. Modern Analytical Ultracentrifugation, pp. 138-155. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Simulated sedimentation velocity profiles; Dept. of Human Biochemistry/Genetics, Univ. of Texas Medical Branch, 617C Basic Science Building, F-47, Galveston, TX 77555-0647

**Lewis, M. S. Data acquisition and analysis systems for the absorption optical system of the analytical ultracentrifuge. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 126-137. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Model E, overview of data acquisition and analysis systems; Biomedical Engineering and Instrumentation Program, National Center for Research Resources, National Institutes of Health, Bethesda, MD 20892

**Liu, S., Stafford, W. F., III. An optical thermometer for direct measurement of cell temperature in the Beckman Instruments XL-A analytical ultracentrifuge. Anal. Biochem. 224, 199-202 (1995)

Optima XL-A, CoCl(2) temperature-sensitive solution used to monitor cell temperature; 3000 rpm, 450-750 nm; Boston Biomedical Research Institute, 20 Staniford St., Boston MA 02114

**Lollar, P. Heterogeneous, ideal associations at sedimentation equilibrium. Biophys. Chem. 28, 245- 251 (1987)

Analysis of mA + nB = A(m)B(n) heteroassociation; effects of random error and presence of contaminants

**Machtle, W. Future requirements for modern analytical ultracentrifuges. Progress in Colloid & Polymer Science, Vol. 86, pp. 111-118. Edited by H.-G. Kilian, G. Lagaly and W. Borchard. Darmstadt, Steinkopff Verlag, 1991.

Shortcomings of both the Model E and the Optima XL-A discussed

**Machtle, W. Determination of highly resolved particle size distributions in the submicron range by ultracentrifugation. Makromol. Chem., Macromol. Symp. 61, 131-142 (1992)

Optima XL modified with 690-nm red light laser optics; Model L(?) modified with turbidity optics and analytic 8-cell rotor; schematics and photos shown; particle size distributions of Dow polystyrene latex, polybutadiene mixture, and carotenoid pigments (food dyes); some analyses done in H(2)O-D(2)O; Kunststofflaboratorium, BASF Aktiengelsellschaft, D-6700 Ludwigshafen, Germany

**McMeekin, T. L., Marshall, K. Specific volumes of proteins and the relationship to their amino acid contents. Science 116, 142-143 (1952)

**McRorie, D. K., Voelker, P. J. Self-Associating Systems in the Analytical Ultracentrifuge. Fullerton, CA, Beckman Instruments, Inc., 1993.

A primer covering molecular weight determinations by sedimentation equilibrium, nonlinear least-squares analysis, goodness of fit and a rational approach to modeling self-associating systems (Appendix A), tables of partial specific volume, and solvent density

**Minton, A. P. Conservation of signal: a new algorithm for the elimination of the reference concentration as an independently variable parameter in the analysis of sedimentation equilibrium. Modern Analytical Ultracentrifugation, pp. 81-93. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Sedimentation equilibrium data analysis algorithm; Lab. of Biochemical Pharmacology, Natl. Inst. of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892

**Modern Analytical Ultracentrifugation; Acquisition and Interpretation of Data for Biological and Synthetic Polymer Systems. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Comprised of 17 papers mentioning use of both the Optima XL-A and the Model E

**Morris, M. B., Ralston, G. B. Biophysical characterization of membrane and cytoskeletal proteins by sedimentation analysis. Subcellular Biochemistry, Vol. 23, pp. 25-82. Edited by H. J. Hilderson and G. B. Ralston. New York, Plenum Press, 1994.

Optima XL-A and Model E described; overview of sedimentation analysis methods; Dept. of Biochemistry, The Univ. of Sydney, Sydney, NSW 2006

**Ogston, A. G. On the variation of the sedimentation rate of spherical particles with concentration. J. Phys. Chem. 65, 51-53 (1961)

**Pavlov, G., Frenkel, S. Sedimentation parameter of linear polymers. Progress in Colloid & Polymer Science, Vol. 99, pp. 101-108. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

The relationship between the sedimentation coefficient and its concentration coefficient obtained by sedimentation velocity is discussed.; Institute of Physics Univ., Ulyanovskaya 1 Petergof, St. Petersburg 198904, Russia

**Perkins, S. J. Protein volumes and hydration effects. The calculation of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157, 169-180 (1986)

**Petrus, V., Bohdanecky, M., Bareiss, R. E. The effect of polymolecularity on the determination of the weight average sedimentation coefficient. Poly. Commun. 31, 68-70 (1990)

Sedimentation velocity theory

**Philo, J. S. Measuring sedimentation, diffusion, and molecular weights by direct fitting of sedimentation velocity concentration profiles. Modern Analytical Ultracentrifugation, pp. 156-170. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Optima XL-A, sed. vel., D, m, S; recombinant brain-derived neurotrophic growth factor, transforming growth factor alpha and bovine serum albumin; Protein Chemistry Dept. 14-2-A-223, Amgen, Inc., Amgen, Inc., Amgen Center, Thousand Oaks, CA 91320

**Prakash, V., Timasheff, S. N. Calculation of partial specific volumes of proteins in 8 M urea solutions. Methods in Enzymology, Vol. 117, pp. 53-60. Edited by C. H. W. Hirs and S. N. Timasheff. New York, Academic Press, 1985.

**Ralston, G. B., Teller, D. C., Bukowski, T. The use of metrizamide for stabilizing against convection in sedimentation equilibrium. Anal. Biochem. 178, 198-201 (1989)

Model E, interference optics, metrizamide used to prevent thermal convection during sedimentation equilbrium of spectrin

**Ralston, G. The renaissance of the analytical ultracentrifuge. Today's Life Sci. 3:12, 42-50 (Dec. 1991)

Overview of analytical ultracentrifugation; photos of Model E and Optima XL-A; brief discussions of applications: molecular weight determination, associating systems, sample purity, conformation changes, density gradient, study of crowding effects; description of XL-A; author is at the Dept. of Biochemistry, Univ. of Sydney

**Ralston, G. Introduction to Analytical Ultracentrifugation. Fullerton, CA, Beckman Instruments, Inc., 1993.

A primer of theory, methods, and applications of the Optima XL-A

**Ralston, G. Analytical ultracentrifugation. Lab. News, 18-19, 22 (March 1994)

Introductory-level article;Optima XL-A is briefly described; Univ. of Sydney, Australia

**Ralston, G. B., Morris, M. B. The use of the omega function for sedimentation equilibrium analysis. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 253-274. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Discussion of omega function for analysis of sed. equil. data for self-associating molecules; tests for heterogeneity; extrapolation to infinite dilution; nonideality; activity coefficients; Dept. of Biochemistry, The Univ. of Sydney, Sydney, NSW 2006, Australia

**Reynolds, J. A., Tanford, C. Determination of molecular weight of the protein moiety in protein-detergent complexes without direct knowledge of detergent binding. Proc. Natl. Acad. Sci. 73, 4467-4470 (1976)

**Rhodes, D. G., Laue, T. M. Determination of purity. Methods in Enzymology, Vol. 182, pp. 555-565. Edited by M. P. Deutscher. San Diego, Academic Press, 1990.

Overview of several methods, including analytical ultracentrifugation

**Richards, E. G., Schachman, H. K. A differential ultracentrifuge technique for measuring small changes in sedimentation coefficients. J. Am. Chem. Soc. 79, 5324-5325 (1957)

**Rivas, G., Minton, A. P. New developments in the study of biomolecular associations via sedimentation equilibrium. Trends Biochem. Sci. 18, 284-287 (1993)

Optima XL-A, Model E, Brandel FR-115 Microfractionator mentioned and briefly described as sedimentation equilibrium methods for studies of macromolecular associations; (Rivas) Dept. of Biophysical Chemistry, Biocenter of the Univ. of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

**Roark, D. E. Sedimentation equilibrium techniques: multiple speed analyses and an overspeed procedure. Biophys. Chem. 5, 185-196 (1976)

**Roark, D. E., Yphantis, D. A. Studies of self-associating systems by equilibrium ultracentrifugation. Ann. N. Y. Acad. Sci. 164, 245-278 (1969)

**Rowe, A. J. The concentration dependence of sedimentation. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 394-406. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Determination of K(s); sedimentation velocity theory; estimation of M(r) from s and k(s); National Centre for Macromolecular Hydrodynamics, Univ. of Leicester, Leicester LE1 7RH, U.K.

**Rowe, A. J., Jones, S. W., Thomas, D. G., Harding, S. E. Methods for off-line analysis of sedimentation velocity and sedimentation equilibrium patterns. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 49-62. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Model E, MSE Mk II or MSE Centriscan mentioned; data analysis for interference and schlieren optics; National Centre for Macromolecular Hydrodynamics, Univ. of Leicester, Leicester LE1 7RH, U.K.

**Roxby, R. W. Sedimentation analysis of micelle-forming systems. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 609-618. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation equilibrium and sedimentation velocity of micellar systems; Dept. of Biochemistry, Microbiology and Molecular Biology, Univ. of Maine, Orono, Maine 04469

**Schachman, H. K. Is there a future for the ultracentrifuge? Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 3-15. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

History of analytical ultracentrifugation; Dept. of Molecular and Cell Biology, W. M. Stanley Hall, Univ. of California, Berkeley, CA 94720

**Scholte, T. G. Molecular weights and molecular weight distribution of polymers by equilibrium ultracentrifugation. Part I. Average molecular weights. J. Polym. Sci., Pt. A-2, 6, 91-109 (1968)

**Schuck, P. Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge. Progress in Colloid & Polymer Science, Vol. 94, pp. 1-13. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil., extinction profiles, M(r); human erythrocyte band 3 protein, DBDS nonionic detergent and oxyhemoglobin mixtures studied as model systems; 11-12,500 rpm; mathematical analysis described; 4deg.C, 270-340 nm; Institut fur Biophysik der Johann Wolfgang Goethe-Universitat and Max-Planck-Institut fur Biophysik, Frankfurt am Main, FRG

**The Scientist. Analytical ultracentrifuges: a 'reinvention'. Scientist 6:22, 18, 20 (Nov. 8, 1992)

Optima XL-A applications described by Preston Hensley, Allen Minton and Howard Schachman

**Stafford, W. F., III. Boundary analysis in sedimentation transport experiments: a procedure for obtaining sedimentation coefficient distributions using the time derivative of the concentration profile. Anal. Biochem. 203, 295-301 (1992)

Model E, interference optics, sed. vel., g*(s); antigen-antibody complex; computation procedure for obtaining sedimentation coefficient distributions from the time derivative of the sedimentation velocity concentration profile; increases signal-to-noise ratio > 10-fold

**Stafford, W. F., III. Methods for obtaining sedimentation coefficient distributions. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 359-393. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Data acquisition and computations for g*(s) determination; extrapolation procedures for one-, two-, and four-component systems; Dept. Muscle Research, Boston Biomedical Research Institute, 20 Staniford Street, Boston, MA 02114

**Stafford, W. F., III. Boundary analysis in sedimentation velocity experiments. Methods in Enzymology, Vol. 240, pp. 478-501. Edited by M. L. Johnson and L. Brand. San Diego, Academic Press, 1994.

Optima XL-A, procedures for sedimentation velocity data analysis; g(s*); Analytical Centrifugation Research Laboratory, Boston Biomedical Research Institute, Boston, MA 02114

**Stafford, W. F., III. Sedimentation boundary analysis of interacting systems: use of the apparent sedimentation coefficient distribution function. Modern Analytical Ultracentrifugation, pp. 119-137. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Use of g(s*) determination; Analytical Centrifugation Research Laboratory, Boston Biomedical Research Institute, Boston, MA 02114

**Stafford, W. F., Liu, S. Methods for increasing the sensitivity of sedimentation velocity analysis: a signal averaging Rayleigh optical system for the Beckman Instruments Optima XL-A Analytical Ultracentrifuge. Proc. SPIE Int. Soc. Opt. Eng. 2386, 130-135 (1995)

Optima XL-A with video-based on-line Rayleigh interference optical system described; Analytical Centrifugation Research Laboratory, Boston Biomedical Research Institute, Boston, MA 02114

**Stafford, W. F., Schuster, T. M. Hydrodynamic methods. Introduction to Biophysical Methods for Protein and Nucleic Acid Research, pp. 111-145. Edited by J. A. Glasel and M. P. Deutscher. San Diego, Academic Press, 1995.

An introductory article discussing analytical ultracentrifugation, sucrose density gradient centrifugation and viscometry; no specific instruments mentioned; Boston Biomedical Research Institute, Boston, MA 02114

**Stafford, W. F., Liu, S., Prevelige, P. E. New high sensitivity sedimentation methods: application to the analysis of the assembly of bacteriophage P22. Techniques in Protein Chemistry, Vol. 6, pp. 427-434. Edited by J. W. Crabb. San Diego, Academic Press, 1995.

Optima XL-A with both absorption and video-based on-line interference optics, g(s*) vs. s*; bacteriophage P22 coat protein-bisANS dye interaction; Analytical Centrifugation Research Laboratory, Boston Biomedical Research Institute, Boston, MA 02114

**Steele, J. H. C., Jr., Tanford, C., Reynolds, J. A. Determination of partial specific volumes for lipid-associated proteins. Methods in Enzymology, Vol. 48, pp. 11-23. Edited by C. H. W. Hirs and S. N. Timasheff. New York, Academic Press, 1978.

**Steinmeier, D. Computer analysis of ultracentrifugation interference patterns. Progress in Colloid & Polymer Science, Vol. 94, pp. 116-119. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Computer program for analysis of digitized interferograms; Univ. of Osnabruck, FRG

**Suzuki, H. Sedimentation analysis of synthetic polymers. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 568-592. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Theory for sedimentation velocity and sedimentation equilibrium studies of nonideal, polydisperse systems; Dept. of Bioengineering, Nagaoka Univ. of Technology, Nagaoka, Niigata-Ken 940-21, Japan

**Teller, D. C., Swanson, E., De Haen, C. The translational friction coefficient of proteins. Methods in Enzymology, Vol. 61, pp. 103-124. Edited by C. H. W. Hirs and S. N. Timasheff. New York, Academic Press, 1979.

**Voelker, P., McRorie, D. alpha-Chymotrypsin: characterization of a self-associating system in the analytical ultracentrifuge. Technical Information T-1782A. Fullerton, Calif., Beckman Instruments, Inc., 1994.

Optima XL-A, sed. equil., K; alpha-chymotrypsin self-association; effect of concentration; Beckman Instruments, Inc., 1050 Page Mill Rd., Palo Alto, CA 94304

**Waxman, E., Laws, W. R., Laue, T. M., Ross, J. B. A. Refining hydrodynamic shapes of proteins: the combination of data from analytical ultracentrifugation and time-resolved fluorescence anisotropy decay. Modern Analytical Ultracentrifugation, pp. 189-205. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Hydrodynamic parameter calculation; Dept. of Biochemistry, Mount Sinai School of Medicine of the City of Univ. of New York, New York 10029

**Williams, J. W., Van Holde, K. E., Baldwin, R. L., Fujita, H. The theory of sedimentation analysis. Chem. Rev. 58, 715-806 (1958)

**Wills, P. R., Winzor, D. J. Thermodynamic non-ideality and sedimentation equilibrium. Analytical Ultracentrifugation in Biochemistry and Polymer Science, pp. 311-330. Edited by S. E. Harding, A. J. Rowe and J. C. Horton. Cambridge, Royal Society of Chemistry, 1992.

Sedimentation equilibrium theory of nonideal solutions; virial and activity coefficients; interacting systems; (Wills) Dept. of Physics, Univ. of Auckland, Auckland, New Zealand

**Wills, P. R., Comper, W. D., Winzor, D. J. Thermodynamic nonideality in macromolecular solutions: interpretation of virial coefficients. Arch. Biochem. Biophys. 300, 206-212 (1993)

(Winzor) Dept. of Biochemistry, Univ. of Queensland, Brisbane, Queensland 4072, Australia

**Winzor, D. J., Wills, P. R. The omega analysis and the characterization of solute self-association by sedimentation equilibrium. Modern Analytical Ultracentrifugation, pp. 66-80. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Sedimentation equilibirum data analysis; Dept.of Biochemistry, Univ. of Queensland, Queensland 4072, Australia

**Yphantis, D. A. Equilibrium ultracentrifugation of dilute solutions. Biochemistry 3, 297-317 (1964)

**Yphantis, D. A., Waugh, D. F. Ultracentrifugal characterization by direct measurement of activity. I. Theoretical. J. Phys. Chem 60, 623-629 (1956)

**Yphantis, D. A., Lary, J. W. Modern equilibrium ultracentrifugation: applications of automated interferometry. Proc. SPIE Int. Soc. Opt. Eng. 2136, 193-204 (1994)

Model E with automated interference optics; methodology and data analysis described; Dept. of Molecular and Cell Biology and National Analytical Ultracentrifuge Facility, Univ. of Connecticut, Storrs, CT 06269-3125

**Yphantis, D. A., Lary, J. W., Stafford, W. F., Liu, S., Olsen, P. H., Hayes, D. B., Moody, T. P., Ridgeway, T. M., Lyons, D. A., Laue, T. M. On line data acquisition for the Rayleigh interference optical system of the analytical ultracentrifuge. Modern Analytical Ultracentrifugation, pp. 209-226. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Model E with conventional and low-magnification interference optics; Dept. of Molecular & Cell Biology and Analytical Ultracentrifugation Facitlity, Univ. of Connecticut, 75 North Eagleville Road, Storrs, CT 06269

Glycoproteins and Proteoglycans

**Borza, D.-B., Tatum, F. M., Morgan, W. T. Domain structure and conformation of histidineñproline-rich glycoprotein. Biochemistry 35, 1925-1934 (1996)

Optima XL-A, sed. vel., S; rabbit plasma histidineñproline-rich glycoprotein and histidineñproline-rich domain; An-60, 40 or 55 krpm, 233 nm, 20 or 25deg.C; effect of pH; CD, PAGE and far UV spectroscopy also used; (Morgan) Div. of Molecular Biology and Biochemistry, School of Biological Sciences, Univ. of Missouri-Kansas City, Kansas City, MO 64110

**Gane, A. M., Craik, D., Munro, S. L. A., Howlett, G. J., Clarke, A. E., Bacic, A. Structural analysis of the carbohydrate moiety of arabinogalactan-proteins from stigmas and styles of Nicotiania alata. Carbohydr. Res. 277, 67-85 (1995)

Optima XL-A, sed. equil., m; Nicotiana alata arabinogalactan-proteins; 5 krpm, 230 nm, 20deg.C; gel filtration and NMR also used; (Bacic) Plant Cell Biology Research Ctr., School of Botany, Univ. of Melbourne, Parkville, Victoria 3052, Australia

**Harding, S. E. Sedimentation equilibrium analysis of glycopolymers. Progress in Colloid & Polymer Science, Vol. 94, pp. 54-65. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Overview of sedimentation equilibrium methods for determining molar mass of glycoconjugates and polysaccharides using schlieren or interference optics; Univ. of Nottingham, School of Agriculture, Sutton Bonington, UK

**Liu, J., Laue, T. M., Choi, H. U., Tang, L.-H., Rosenberg, L. The self-association of biglycan from bovine articular cartilage. J. Biol. Chem. 269, 28366-28373 (1994)

Optima XL-A with interference optics, sed. vel., g (s*); Model E with schlieren optics, sed. vel., S; Model E with interference optics, sed. equil., M(z); effect of concentration and GuHCl on state of association; beef cartilage dermatan sulfate proteoglycan; (Laue) Dept. Biochem. and Mol. Biol., Univ. of New Hampshire, Durham, NH 03824

**Shire, S. J. Determination of molecular weight of glycoproteins by analytical ultracentrifugation. Technical Information DS-837. Palo Alto, Calif., Beckman Instruments, Inc., Spinco Business Unit, 1992.

Optima XL-A, sed. equil., M; recombinant HIV-1 envelope glycoprotein, human tumor necrosis factor receptor; 10 krpm and 280 nm or 15 krpm, 232 nm, 20 ; Dept. of Pharmaceutical R&D, Genentech, Inc., 460 Point San Bruno Blvd., South San Francisco, CA 94080

**Shire, S. J. Analytical ultracentrifugation and its use in biotechnology. Modern Analytical Ultracentrifugation, pp. 261-297. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Optima XL-A, sed. equil., M; recombinant HIV-1 envelope glycoprotein, recombinant apolipoprotein A, and human tumor necrosis factor type 1 receptor and its TNF-alpha complex; 5, 10 or 15 krpm; Dept. of Pharmaceutical R&D, Genentech, Inc., 460 Point San Bruno Blvd., South San Francisco, CA 94080

**Zhuang, P., Blackburn, M. N., Peterson, C. B. Characterization of the denaturation and renaturation of human plasma vitronectin. I. Biophysical characterization of protein unfolding and multimerization. J. Biol. Chem. 271, 14323-14332 (1996)

Optima XL-A, sed. equil., M(r), state of oligomerization; sed. vel., S; human plasma vitronectin and multimers; 10-20 krpm (s.e), 60 krpm (s.v.); 280 nm, 20deg.C; effect of urea or GuHCl; CD and fluorescence also used; (Peterson) M407 Walters Life Sciences Bldg., Dept. of Biochemistry and Cellular and Molecular Biology, Univ. of Tennessee, Knoxville, TN 37996

Lipoproteins

**Fless, G. M., Snyder, M. L., Furbee, J. W., Jr., Garcia-Hedo, M.-T., Mora, R. Subunit composition of lipoprotein(a) protein. Biochemistry 33, 13492-13501 (1994)

Optima XL-A, sed. equil., b.d., M(r); human plasma LDL, lipoprotein(a), reduced and carboxymethylated of apolipoproteins(a) and -(b), and apoB-apo(a) complex; 3-10 krpm, density adjusted with NaBr; GuHCl; (Fless) Dept. of Medicine, Univ. of Chicago, 5841 S. Maryland Ave., Chicago, IL 60637

**Fless, G. M., Furbee, J., Jr., Snyder, M. L., Meredith, S. C. Ligand-induced conformational change of lipoprotein(a). Biochemistry 35, 2289-2298 (1996)

Optima XL-A, sed. equil. in NaBr, M(r), v-bar; sed. vel., D, f/f(0), K(d), R(s), S; human LDL, Lp(a), and Lp(a-)ñ6-aminohexanoic acid complexes; rhesus monkey Lp(a) and its 6-AHA complex; An-60 Ti; 40 krpm (s.v.), 3500 rpm (diff.), 220 or 280 nm; effect of concentration; PAGE also used; Dept. of Medicine, Univ. of Chicago, 5841 S. Maryland Ave., Chicago, IL 60637

**Kawabe, Y., Cynshi, O., Takashima, Y., Suzuki, T., Ohba, Y., Kodama, T. Oxidation-induced aggregation of rabbit low-density lipoprotein by azo initiator. Arch. Biochem. Biophys. 310, 489-496 (1994)

Optima XL-A, sed. vel., S; rabbit oxidized, aggregated or monomeric, or acetylated low density lipoproteins; XL-80, AN-60 Ti, 10 or 50 krpm, 280 nm; LS & GPC also used; (Cynshi) Fujigotemba Research Laboratories Chugai Pharmaceutical Co., Ltd., 1-135 Komakado, Gotemba-shi, Shizuoka 412, Japan

Miscellaneous Samples (Including Peptides)

**Atkins, A. R., Martin, R. C., Smith, R. (1)H NMR studies of sarafotoxin SRTb, a nonselective endothelin receptor agonist, and IRL 1620, an ET(B) receptor-specific agonist. Biochemistry 34, 2026-2033 (1995)

Optima XL-A, sed. equil., state of association; receptor-specific agonist peptide; 60 krpm, 280 & 360 nm, 7 & 20deg.C; NMR & CD also; Biochemistry Dept., Univ. of Queensland, Queensland 4072, Australia

**Betz, S. F., DeGrado, W. F. Controlling topology and native-like behavior of de novo-designed peptides: design and characterization of antiparallel four-stranded coiled coils. Biochemistry 35, 6955-6962 (1996)

Optima XL-A, sed, equil., delta G, K; synthetic coiled-coil peptides; 35, 42 and 48 krpm; CD, fluorescence and NMR also used; (DeGrado) The Johnson Research Foundation, Dept. of Biochemistry and Biophysics, Univ. of Pennsylvania, Philadelphia, PA 19104-6059

**Blacklow, S. C., Lu, M., Kim, P. S. A trimeric subdomain of the simian immunodeficiency virus envelope glycoprotein. Biochemistry 34, 14955-14962 (1995)

Optima XL-A, sed. equil., m, state of oligomerization; recombinant SIV envelope glycoprotein domain peptides and their trimeric complex; An-60 Ti, 13-20 krpm, 20deg.C, CD also used; (Kim) Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Dept. of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142

**Blanco, F. J., Rivas, G., Serrano, L. A short linear peptide that folds into a native stable beta-hairpin in aqueous solution. Nature, Struct. Biol. 1, 584-590 (1994)

Optima XL-A, sed. equil., M(w); synthetic 16-residue peptide monomer; An-60 Ti, 40 krpm; CD, NMR & SEC also used; (Blanco) EMBL, Postfach 102209, Meyerhofstrasse 1, 69012 Heidelberg, Germany

**Carr, C. M., Kim, P. S. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell 73, 823-832 (1993)

Optima XL-A, sed. equil., M; synthetic coiled-coil peptide corresponding to influenza virus hemagglutinin peptide; 22 & 27 krpm, pH 7.2 & 4.7; Howard Hughes Medical Institute, Whitehead Institute for Biomedical Research, Dept. of Biology, Massachusetts Institute of Technology, Cambridge, MA 02142

**C^lfen, H., Harding, S. E.. A study on Schlieren patterns derived with the Beckman Optima XL-A UV-absorption optics. Progress in Colloid & Polymer Science, Vol. 99, pp. 167-186. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A, sed. vel., schlieren effect derived with absorption optics used to examine various polysaccharides: chitosan, kappa-carrageenan, Na-alginate, dextrans 20 and 150, and xanthan; 12.6-60 krpm, 20deg.C, 276-600 nm; results compared to Model E with schlieren optics; Max-Planck-Inst. for Colloid and Interface Research, Colloid Chemistry Dept., Kantstrasse 55, 14513 Teltow, Germany

**Dhami, R., C^lfen, H., Harding, S. E. A comparative "Schlieren" study of the sedimentation behaviour of three polysaccharides using the Beckman Optima XL-A and Model E analytical ultracentrifuges. Progress in Colloid & Polymer Science, Vol. 99, pp. 187-192. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A schlieren effect results compared with Model E schlieren results, sed. vel., K(s), S; polysaccharides: arabinoxylan, xanthan and locust bean gum; 30 or 60 krpm, 200-600 nm, 20deg.C; (Harding) Natl. Ctr. for Macromolecular Hydrodynamics, Univ. of Nottingham, Sutton Bonington Campus, Loughborough LE12 5RD, UK

**Dhami, R., Harding, S. E., Elizabeth, N. J., Ebringerova, A. Hydrodynamic characterisation of the molar mass and gross conformation of corn cob heteroxylan AGX. Carbohydr. Polym. 28, 113-119 (1995)

Optima XL-A used to obtain schlieren diagrams, sed. vel., S; Model E, interference optics, sed. equil., M(w); MSE MkII analytical ultracentrifuge, schlieren optics, sed. equil., M(z); corn cob heteroxylan; 60 krpm (s.v.); 440 nm used for schlieren method; 20deg.C; 6000 rpm (s.e.), 20deg.C; viscometry also used; Univ. of Nottingham, Natl. Ctr. for Macromolecular Hydrodynamics, Dept. of Applied Biochemistry and Food Science, Sutton Bonington, LE12 5RD, UK

**Digard, P., Williams, K. P., Hensley, P., Brooks, I. S., Dahl, C. E., Coen, D. M. Specific inhibition of herpes simplex virus DNA polymerase by helical peptides corresponding to the subunit interface. Proc. Natl. Acad. Sci. 92, 1456-1460 (1995)

Optima XL-A, sed. equil., m, v-bar; synthetic DNA polymerase catalytic subunit 36-residue peptide; 50 or 60 krpm, 230 nm; H(2)O or D(2)O; CD also used; (Coen) Dept. of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115

**D^beli, H., Draeger, N., Huber, G., Jakob, P., Schmidt, D., Seilheimer, B., Stuber, D., Wipf, B., Zulauf, M. A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide. Bio/Technology 13, 988-993 (1995)

Optima XL-A, sed. equil., m; recombinant Alzheimer's beta-amyloid peptide; 40 krpm; CD, mass spectrometry, PAGE and size exclusion chromatography also used; Pharma Division, Preclinical Research, F. Hoffmann-La Roche, CH-4002 Basel, Switzerland

**Fairman, R., Chao, H.-G., Mueller, L., Lavoie, T. B., Shen, L., Novotny, J., Matsueda, G. R. Characterization of a new four-chain coiled-coil: influence of chain length on stability. Protein Sci. 4, 1457-1469 (1995)

Optima XL-A, sed. equil., state of oligomerization; synthetic coiled-coil peptide monomers-tetramers; An-60 Ti, 20, 30, and 40 krpm, 240 nm, 25deg.C; CD and gel filtration also used; effect of speed; Div. of Macromolecular Structure, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ, 08543-4000

**Fairman, R., Chao, H.-G., Lavoie, T. B., Villafranca, J. J., Matsueda, G. R., Novotny, J. Design of heterotetrameric coiled coils: evidence for increased stabilization by Gly(-)-Lys(+) ion pair interactions. Biochemistry 35, 2824-2829 (1996)

Optima XL-A, sed. equil., M, state of oligomerization; synthetic coiled-coil peptides and heterotetramers; An-60 Ti, 30, 40 and 50 krpm, 242 nm, 25deg.C; CD also used; Div. of Macromolecular Structure, Bristol-Myers Squibb Pharmaceutical Research inst., P.O. 4000, Princeton, NJ 08543-4000

**Farr, C. D., Galiano, F. J., Witt, S. N. Large activation energy barriers to chaperone-peptide complex formation and dissociation. Biochemistry 34, 15574-15582 (1995)

Optima XL-A, sed. equil., M, state of association; dansylated and unlabeled synthetic Cro repressor protein peptides; 40 krpm, 275 and 335 nm, 25deg.C; fluorescence and SEC also used; (Witt) Dept. of Biochemistry and Molecular Biology, Louisiana State Univ. Medical Center, 1501 Kings Highway, Shreveport, LA 71130-3932

**Fletcher, T. M., Hansen, J. C. Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J. Biol. Chem. 270, 25359-25362 (1995)

Optima XL-A, sed. vel., S; chicken erythrocyte trypsinized nucleosomal arrays; effect of MgCl(2) concentration; (Hansen) Dept. of Biochemistry, Univ. of Texas Health Science Center, 7703 Floyd Curl Dr., San Antonio, TX 78284-7760

**Fletcher, T. M., Krishnan, U., Serwer, P., Hansen, J. C. Quantitative agarose gel electrophoresis of chromatin: nucleosome-dependent changes in charge, shape, and deformability at low ionic strength. Biochemistry 33, 2226-2233 (1994)

Optima XL-A, sed. vel., s distribution; chicken erythrocyte nucleosomal arrays; An-60 Ti, 18-28 krpm; (Hansen) Dept. of Biochemistry, The Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7760

**Fletcher, T. M., Serwer, P., Hansen, J. C. Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: application to chromatin folding. Biochemistry 33, 10859-10863 (1994)

Optima XL-A, sed. vel., S; DNA and nucleosomal arrays; Dept. of Biochemistry, Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7760

**Germeroth, L., Lottspeich, F., Robert, B., Michel, H. Unexpected similarities of the B800-850 light-harvesting complex from Rhodospirillum molischianum to the B870 light-harvesting complexes from other purple photosynthetic bacteria. Biochemistry 32, 5615-5621 (1993)

Optima XL-A (inferred), sed. equil., M; bacteria light-harvesting complex II (B800/850); no exptl. details; SDS-PAGE also used; Michel) Max-Planck-Institut fur Biophysik, Abteilung Molekulare Membranbiologie, 6000 Frankfurt, FRG

**Gibbons, D. L., Horowitz, P. M. Exposure of hydrophobic surfaces on the chaperonin GroEL oligomer by protonation or modification of His-401. J. Biol. Chem. 270, 7335-7340 (1995)

Optima XL-A, sed. vel., S; recombinant chaperonin GroEL oligomer; An-60 Ti, 20 or 27 krpm, effect of pH 5.5; fluorescence also used; 14-mer; Dept. of Biochemistry, Univ. of Texas Health Science Center, San Antonio, TX 78284-7760

**Giordano, T., Pan, J. B., Monteggia, L. M., Holzman, T. F., Snyder, S. W., Krafft, G., Ghanbari, H., Kowall, N. W. Similarities between beta amyloid peptides 1-40 and 40-1: effects on aggregation, toxicity in vitro, and injection in young and aged rats. Exp. Neurol. 125, 175-182 (1994)

Optima XL-A, sed. vel., aggregation detected and related to toxicity; synthetic beta-amyloid peptides; 30 krpm; (Giordano) Abbott Laboratories, Dept. of Neuroscience, Abbott Park, IL 60064

**Gonzalez, L., Jr., Plecs, J. J., Alber, T. An engineered allosteric switch in leucine-zipper oligomerization. Nat. Struct. Biol. 3, 510-515 (1996)

Optima XL-A, sed. equil., M(r), state of oligomerization; coiled-coil leucine zipper peptides and ligand complexes; 50 krpm, 235 and 220 nm, 5deg.C and 25deg.C; effect of benzene; CD also used; (Alber) Dept. of Molecular and Cell Biology, 229 Stanley Hall, Univ. of California, Berkeley, CA 94720-3206

**Hansen, J. C., Wolffe, A. P. A role for histones H2A/H2B in chromatin folding and transcriptional repression. Proc. Natl. Acad. Sci. 91, 2339-2343 (1994)

Optima XL-A, sed. vel., s distributions; reconstituted nucleosomal arrays; effect of Mg(2+) concentration; (Hansen) Dept. of Biochemistry, Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78284-7760

**Harbury, P. B., Zhang, T., Kim, P. S., Alber, T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 262, 1401-1407 (1993)

Optima XL-A, sed. equil., M; effect of pH and concentration on synthetic coiled-coil peptides; An-60 Ti, various rotor speeds; (Alber) Dept. of Molecular and Cell Biology, Univ. of California, Berkeley, CA 94720

**Harding, S. E. Sedimentation equilibrium analysis of glycopolymers. Progress in Colloid & Polymer Science, Vol. 94, pp. 54-65. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Overview of sedimentation equilibrium methods for determining molar mass of glycoconjugates and polysaccharides using schlieren or interference optics; Univ. of Nottingham, School of Agriculture, Sutton Bonington, UK

**Harding, S. E. Some recent developments in the size and shape analysis of industrial polysaccharides in solution using sedimentation analysis in the analytical ultracentrifuge. Carbohydr. Polym. 28, 227-237 (1995)

Overview of sedimentation equilibrium and velocity methods, and review of applications; Optima XL-I mentioned; Univ. of Nottingham, Dept. of Applied Biochemistry and Food Science, Sutton Bonington LE12 5RD, UK

**Hedges, J., Sarrafzadeh, S., Lear, J. D., McRorie, D. K. Extensions to commercial graphics packages for customization of analysis of analytical ultracentrifuge data. Modern Analytical Ultracentrifugation, pp. 227-244. Edited by T. M. Schuster and T. M. Laue. Boston, Birkhauser, 1994.

Optima XL-A data analysis using extended Originô (MicroCal Software, Inc.) software; examples of sedimentation equilibrium data analysis of coiled-coil Trp peptide given; Beckman Instruments, Inc., 1050 Page Mill Road, Palo Alto, CA 94304

**Joslyn, G., Richardson, D. S., White, R., Alber, T. Dimer formation by an N-terminal coiled coil in the APC protein. Proc. Natl. Acad. Sci. 90, 11109-11113 (1993)

Optima XL-A, sed. equil., M(r); familial adenomatous polyposis APC gene product coiled-coil peptides; 235 or 280 nm; (Alber) Dept. of Molecular and Cell Biology, Stanley/Donner ASU, Univ. of California, Berkeley, CA 94720

**Kojima, S., Kuriki, Y., Sato, Y., Arisaka, F., Kumagai, I., Takahashi, S., Miura, K. Synthesis of alpha-helix-forming peptides by gene engineering methods and their characterization by circular dichroism spectra measurements. Biochim. Biophys. Acta 1294, 129-137 (1996)

Optima XL-A, sed. equil., M, state of oligomerization; recombinant alpha-helix-forming peptides; An-60 Ti, 20 krpm, 230 nm, 20deg.C; CD and gel filtration also used; state of oligomerization; (Miura) Inst. for Biomolecular Science, Gakushuin Univ., Mejiro, Tokyo 171, Japan

**Lewis, M. S., Shrager, R., Kim, S. J. Ultracentrifugal analysis of protein-nucleic acid interactions using multi-wavelength scans. Progress in Colloid & Polymer Science, Vol. 94, pp. 46-53. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil., absorbancy distributions at multiple wavelengths; Drosophila heat shock factor polypeptide, synthetic oligodeoxynucleotide and their interaction; 230-246, 260 & 280 nm; (Lewis) Biomedical Engineering and Instrumentation Program, National Center for Research Resources, Bethesda, MD

**Linsdell, H., Toiron, C., Bruix, M., Rivas, G., Menendez, M. Dimerization of A82846B, vancomycin and ristocetin: influence on antibiotic complexation with cell wall model peptides. J. Antibiot. 49, 181-193, (1996)

Optima XL-A, sed. equil., K; glycopeptide antibiotics A82846B, vancomycin and ristocetin and their cell wall model peptide complexes; 40 krpm; 240, 280 and 300 nm; 25deg.C; NMR also used; Instituto "Rocasolano", Serrano 119, Spain

**Lovejoy, B., Choe, S., Cascio, D., McRorie, D. K., DeGrado, W. F., Eisenberg, D. Crystal structure of a synthetic triple-stranded alpha-helical bundle. Science 259, 1288-1293 (1993)

Optima XL-A, sed. equil., m; synthetic coil-Ser peptide; 30 krpm; Mol. Biol. Inst. & Dept. of Chemistry & Biochemistry, Univ. California at Los Angeles; Beckman Instruments, Palo Alto; Biotechnolgy Dept., DuPont Merck Pharmaceuticals Co., Wilmington, DE

**Montoya, G., Cyrklaff, M., Sinning, I. Two-dimensional crystallization and preliminary structure analysis of light harvesting II (B800-850) complex from the purple bacterium Rhodovulum sulfidophilum. J. Mol. Biol. 250, 1-10 (1995)

Optima XL-A, sed. equil., M(r); sed. vel., state of association; bacterial light harvesting II complex; 14 krpm (s.e.), 56 krpm (s.v.), 275 or 367 nm, 20deg.C; 1% octyl-POE as detergent; PAGE and gel filtration also used; (Sinning) European Molecular Biology Laboratory, Meyarhofstrasse 1 69012 Heidelberg, Germany

**Nautiyal, S., Woolfson, D. N., King, D. S., Alber, T. A designed heterotrimeric coiled coil. Biochemistry 34, 11645-11651 (1995)

Optima XL-A, sed. equil., m; synthetic peptides and their heterotrimeric coiled coil; 20 and 30 krpm; 229, 276 and 285 nm; 10deg.C; CD and PAGE also used; (Alber) Dept. of Molecular and Cell Biology, 229 Stanley Hall, Univ. of California, Berkeley, CA 94720-3206

**Merutka, G., Morikis, D., Bruschweiler, R., Wright, P. E. NMR evidence for multiple conformations in a highly helical model peptide. Biochemistry 32, 13089-13097 (1993)

Optima XL-A, sed. equil., m; synthetic helical peptide; 35 krpm, 276 nm, CD & NMR also used; worked performed by Paul Voelker, Beckman; Dept. of Molecular Biology, The Scripps Research Institute, 10666 North Torrey Road, La Jolla, CA 92037

**Mills, R. G., Ralston, G. B., King, G. F. The solution structure of sarafotoxin-c. Implications for ligand recognition by endothelin receptors. J. Biol. Chem. 269, 23413-23419 (1994)

Optima XL-A, sed. equil., m, associative state; synthetic sarafotoxin-c peptide monomer; 30-40 krpm, 280 nm, effect of conc.; "oligomeric state necessary for NMR studies"; Dept. of Biochemistry, Univ. of Sydney, Sydney, New South Wales 2006, Australia

**Moore, K. L., Eaton, S. F., Lyons, D. E., Lichenstein, H. S., Cummings, R. D., McEver, R. P. The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine. J. Biol. Chem. 269, 23318-23327 (1994)

Optima XL-A, interference optics, sed. equil., m, sed. vel., S; recombinant truncated soluble E-selectin monomer; 10-25 krpm (s.e.), 60 krpm (s.v.), prototype optics at Univ. of New Hampshire; effect of concentration; axial ratio; (Moore) Dept. of Medicine, Univ. of Oklahoma Health Sciences Center, 825 N. E. 13th St., Oklahoma City, OK 73014

**Morris, M. B., Ralston, G. B., Biden, T. J., Browne, C. L., King, G. F., Iismaa, T. P. Structural and biochemical studies of human galanin: NMR evidence for nascent helical structures in aqueous solution. Biochemistry 34, 4538-4545 (1995)

Optima XL-A, sed. equil., m; synthetic human galanin monomer; 30 krpm, 280, 300 & 360 nm; 20deg.C; CD and NMR also used; 30-residue neuropeptide; Dept. of Biochemistry, Univ. of Sydney, Sydney, Australia

**Muhle-Goll, C., Gibson, T., Schuck, P., Schubert, D., Nalis, D., Nilges, M., Pastore, A. The dimerization stability of the HLH-LZ transcription protein family is modulated by the leucine zippers: a CD and NMR study of TFEB and c-Myc. Biochemistry 33, 11296-11306 (1994)

Optima XL-A, sed. equil., state of association; synthetic TFEB transcription activator protein leucine zipper peptide monomer-dimer; 40 krpm, 4deg.C, 275 nm; (Muhle-Goll) EMBL, Meyerhofstrasse 1, D-69117 Heidelberg, Germany

**Mulhern, T. D., Howlett, G. J., Reid, G. E., Simpson, R. J., McColl, D. J., Anders, R. F., Norton, R. S. Solution structure of a polypeptide containing four heptad repeat units from a merozoite surface antigen of Plasmodium falciparum. Biochemistry 34, 3479-3491 (1995)

Optima XL-A, sed. equil., m; synthetic antigen SPAM monomer; 20, 35 & 40 krpm; 230, 240, 245 & 290 nm; effect of concentration; 38-residue peptide; D(2)O; NMR also; (Norton) Dept. of Medicine, Univ. of Queensland, Princess Alexandra Hospital, Queensland 4102, Australia

**Musco, G., Tziatzios, C., Schuck, P., Pastore, A. Dissecting titin into its structural motifs: identification of an alpha-helix motif near the titin N-terminus. Biochemistry 34, 553-561 (1995)

Optima XL-A, sed. equil., state of association; synthetic titin (connectin) coiled-coil peptide monomer-tetramer; An-60 Ti, 35 & 25 krpm, 275 nm; 38-residues; CD & NMR also; effect of pH & salt conc.; EMBL, Meyerhofstrasse 1, W-69012 Heidelberg, Germany

**Myszka, D. G., Chaiken, I. M. Design and characterization of an intramolecular antiparallel coiled coil peptide. Biochemistry 33, 2363-2372 (1994)

Optima XL-A, sed. equil., m; synthetic coiled-coil stem loop peptide; 40 krpm, 235 nm, 4deg.C; used to confirm monomer m determined by gel/filtration; CD & MS also used; SmithKline Beecham Research and Development, 709 Swedeland Road, UE0548, King of Prussia, PA 19406-2799

**Needham, G. F., Pekar, A. H., Havel, H. A. Effect of salts on the structure of a potent analog of growth hormone releasing hormone as determined by optical spectroscopy. J. Pharm. Sci. 84, 437-442 (1995)

Optima XL-A, sed. equil., effect of urea on state of association; synthetic growth hormone analog; An-60 Ti, 22 krpm, 280 nm, 22deg.C; effect of urea; CD and light scattering also used; Eli Lilly and Co., P.O. B. 708 Greenfield, IN 46140

**O'Shea, E. K., Lumb, K. J., Kim, P. S. Peptide 'Velcro': design of a heterodimeric coiled coil.

Curr. Biol. 3, 658-667 (1993)

Optima XL-A, sed. equil., state of association; synthetic leucine zipper region coiled-coil peptide heterodimers; 30-40 krpm; CD & NMR also used; (Kim) Dept. of Biology, Massachusetts Institute of Technology, Nine Cambridge Center, Cambridge, MA 02142

**Rabenstein, M., Shin, Y.-K. A peptide from the heptad repeat of human immunodeficiency virus gp41 shows both membrane binding and coiled-coil formation. Biochemistry 34, 13390-13397 (1995)

Optima XL-A, sed, equil., m, state of oligomerization; HIV envelope glycoprotein coiled-coil peptide; 40 krpm, effect of concentration; CD and EPR also used; (Shin) Dept. of Chemistry, Univ. of California, Berkeley, CA 94720

**Sabharwal, A. K., Birktoft, J. J., Gorka, J., Wildgoose, P., Petersen, L. C., Bajaj, S. P. High affinity Ca(2+)-binding site in the serine protease domain of human factor VIIa and its role in tissue factor binding and development of catalytic activity. J. Biol. Chem. 270, 15523-15530 (1995)

Optima XL-A, sed. equil., M(r); synthetic human Factor VIIa peptide; 40 krpm, 22deg.C, 280 nm; effect of salt; CD and PAGE also used; (Bajaj) St. Louis Univ. Health Sciences Ctr., 3635 Vista Ave., P.O. Box 15250, St. Louis, MO 63110-0250

**Sakamoto, H., Lewis, M. S., Kodama, H., Appella, E., Sakaguchi, K. Specific sequences from the carboxyl terminus of human p53 gene product form anti-parallel tetramers in solution. Proc. Natl. Acad. Sci. 91, 8974-8978 (1994)

Optima XL-A, sed. equil., K(D), delta G; synthetic p53 gene product peptides association; 24-32 krpm, 5-33deg.C, 231 nm; (Appella) Laboratory of Cell Biology, National Cancer Institute, Bldg. 37, Room 1B10, Bethesda, MD 20892

**Schubert, D., Tziatzios, C., van den Broek, J. A., Schuck, P., Germeroth, L., Michel, H. Determination of the molar mass of pigment-containing complexes of intrinsic membrane proteins: problems, solutions and application to the light-harvesting complex B800/820 of Rhodospirillum molischianum Progress in Colloid & Polymer Science, Vol. 94, pp. 14-19. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil, m,v-bar; Rhodospirillum molischianum light harvesting protein-pigment complex oligomers in various detergent solutions; 15-25 krpm, 357 or 370 nm, 6deg.C; Institut fur Biophysik, JWG-Universitat, Frankfurt am Main, FRG

**Schwartz, P. M., Felthauser, A., Fletcher, T. M., Hansen, J. C. Reversible oligonucleosome self-association: dependence on divalent cations and core histone tail domains. Biochemistry 35, 4009-4015 (1996)

Optima XL-A, sed. vel., S, state of association; chicken erythrocyte oligonucleosomes; 4-28 krpm; effect of Mg(2+) ion; (Hansen) Dept. of Biochemistry, Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78284-7760

**Schwarz, P. M., Hansen, J. C. Formation and stability of higher order chromatin structures. Contributions of the histone octamer. J. Biol. Chem. 269, 16284-16289 (1994)

Optima XL-A, sed. equil., m; sed. vel., S; Model E with Scanner, sed. vel., S; chicken erythrocyte chromatin oligonucleosomes; Dept. of Biochemistry, Univ. of Texas Health Science Center, San Antonio, TX 78284-7760

**Snyder, S. W., Ladror, U. S., Wade, W. S., Wang, G. T., Barrett, L. W., Matayoshi, E. D., Huffaker, H. J., Krafft, G. A., Holzman, T. F. Amyloid-beta aggregation: selective inhibition of aggregation in mixtures of amyloid with different chain lengths. Biophys. J. 67, 1216-1228 (1994)

Optima XL-A, sed. equil., m, sed. vel., S, g*(s); aggregation state; synthetic amyloid-beta 39-43 residue peptide; An-60 Ti, 3000-60 krpm (s.e.), 1000-30,000 krpm; dynamic light scattering & turbidity also used; effect of solvents; oil deposits on optics; (Holzman) D-46Y, AP-10, Protein Biochemistry, Pharmaceutical Discovery Research, Abbott Laboratories, 1 Abbott Park Road, Abbott Park, IL 60064-3500

**Terzi, E., H^lzemann, G., Seelig, J. Reversible random coilñbeta-sheet transition of the Alzheimer beta-amyloid fragment (25-35). Biochemistry 33, 1345-1350 (1994)

Optima XL-A, sed. equil., m; synthetic beta-amyloid peptide; An-60 Ti, 56 krpm; CD also used; Dept. of Biophysical Chemistry, Biocenter of the Univ. of Basel, Klingelbergstrsse 70, CH-4056 Basel, Switzerland

**Terzi, E., H^lzemann, G., Seelig, J. Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252, 633-642 (1995)

Optima XL-A, sed. equil., degree of association, m; commercial beta-amyloid peptide (Alzheimer peptide); 8 or 52 krpm; CD and calorimetry also used; (Seelig) Dept. of Biophysical Chemistry, Biocenter of the Univ. of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland

**Thomas, R. M., Wendt, H., Zampieri, A., Bosshard, H. R. alpha-Helical coiled coils: simple models for self-associating peptide and protein systems. Progress in Colloid & Polymer Science, Vol. 99, pp. 24-30. Edited by J. Behlke. Darmstadt, Steinkopff Verlag, 1995.

Optima XL-A, sed. equil., m; synthetic coiled-coil peptides; 21 krpm, 230 nm, 20deg.C; effect of concentration; CD also used; Institut fur Polymere, ETH-Zentrum, 8092 Zurich, Switzerland

**Tziatzios, C., Schuck, P., Schubert, D., Tsiotis, G. The molar mass of an active photosystem I complex from the cyanobacterium Synechococcus PCC 7002. Z. Naturforsch., C: Biosci. 49, 220-222 (1994)

Optima XL-A, sed. equil., M(r),v-bar; Synechococcus photosystem I complex (protein-pigment complex); D(2)O/D(2)(18) O method for v-bar; effect of three detergents; (Schubert) Institut fur Biophysik der J. W. Goethe-Universitat, Theodor-Stern, Kai 7, Hous 74, D-60590 Frankfurt am Main, Bundesrepublik Deutschland

**Wendt, H., Berger, C., Baici, A., Thomas, R. M., Bosshard, H. R. Kinetics of folding of leucine zipper domains. Biochemistry 34, 4097-4107 (1995)

Optima XL-A, sed. equil., m; synthetic leucine zipper coiled-coil peptides; 16-40 krpm, 20deg.C, FC43 false bottom; fluorescence & stopped-flow also used; Biochemisches Institut der Universitat Zurich, Winterhurerstrasse 190, CH-8057 Zurich, Switzerland

**Wendt, H., Durr, E., Thomas, R. M., Przybylski, M., Bosshard, H. R. Characterization of leucine zipper complexes by electrospray ionization mass spectrometry. Protein Sci. 4, 1563-1570 (1995)

Optima XL-A, sed. equil., m; degree of oligomerization; synthetic leucine zipper coiled coil peptides; 16-42 krpm, 20deg.C; number of strands determined; CD and mass spectrometry also used; (Bosshard) Biochemisches Institut der Universitat Zurich, CH-8057 Zurich, Switzerland

**Yoo, S. H., Lewis, M. S. Dimerization and tetramerization properties of the C-terminal region of chromogranin A: a thermodynamic analysis. Biochemistry 32, 8816-8822 (1993)

Model E with Scanner, Optima XL-A (240 nm), sed. equil., delta G, delta H, delta C, delta S; effect of pH and temperature (2-32deg.C); chromogranin A peptides monomer-dimer & monomer-tetramer equilibria; 30 krpm; CD also; (Yoo) Laboratory of Cellular Biology, NIDCD/NIH, Building 36, Room 5D-15, Bethesda, MD 20892

Nucleic Acids

**Clark, D. J., Ghirlando, R., Felsenfeld, G., Eisenberg, H. Effect of positive supercoiling on DNA compaction by nucleosome cores. J. Mol. Biol. 234, 297-301 (1993)

Optima XL-A, sed. vel., S plotted as a function of mean excess linking number (delta Lk); plasmid DNAs and reconstituted nucleosome cores; 24-25 krpm, 260 nm, Beckman XLAVEL data analysis; Laboratory of Molecular Biology, NIDDK, National Institutes of Health, Bethesda, MD 20892

**Dolinnaya, N. G., Braswell, E. H., Fossella, J. A., Klump, H., Fresco, J. R. Molecular and thermodynamic properties of d(A(+)-G)(10), a single-stranded nucleic acid helix without paired or stacked bases. Biochemistry 32, 10263-10270 (1993)

Optima XL-A, sed. equil., B, M; deoxyoligonucleotide strand; 48, 52 or 40 krpm, FC43 used, 300 & 280 nm, fit to single-species ideal model; 4 or 40deg.C; (Fresco) Dept. of Molecular Biology, Princeton Univ., Princeton, NJ 08544-1014

**Fletcher, T. M., Serwer, P., Hansen, J. C. Quantitative analysis of macromolecular conformational changes using agarose gel electrophoresis: application to chromatin folding. Biochemistry 33, 10859-10863 (1994)

Optima XL-A, sed. vel., S; DNA and nucleosomal arrays; Dept. of Biochemistry, Univ. of Texas Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, TX 78284-7760

**Lewis, M. S., Shrager, R., Kim, S. J. Ultracentrifugal analysis of protein-nucleic acid interactions using multi-wavelength scans. Progress in Colloid & Polymer Science, Vol. 94, pp. 46-53. Edited by M. D. Lechner. Darmstadt, Steinkopf, 1994.

Optima XL-A, sed. equil., absorbancy distributions at multiple wavelengths; Drosophila heat shock factor polypeptide, synthetic oligodeoxynucleotide and their interaction; 230-246, 260 & 280 nm; (Lewis) Biomedical Engineering and Instrumentation Program, National Center for Research Resources, Bethesda, MD

**Rohozinski, J., Hancock, J. M., Keniry, M. A. Polycytosine regions contained in DNA hairpin loops interact via a four-stranded, parallel structure similar to the i-motif. Nucleic Acids Res. 22, 4653-4659 (1994)

Optima XL-A, sed. equil., M(b), effect of pH on state of association; oligodeoxynucleotide and dimer; 40 krpm, 260 nm; CD & NMR also used; (Rohozinski) Research School of Biological Sciences , Australian National Univ., Canberra, ACT 0200, Australia

**Scaria, P. V., Shire, S. J., Shafer, R. H. Quadruplex structure of d(G(3)T(4)G(3)) stabilized by K(+) or Na(+) is an asymmetric hairpin dimer. Proc. Natl. Acad. Sci. 89, 10336-10340 (1992)

Optima XL-A, sed. equil., M; effect of ions on oligonucleotides; 40 krpm, also P/ACE; (Shafer) Dept. of Pharmaceutical Chemistry, School of Pharmacy, Univ. of California, San Francisco, CA 94143.

**Seifert, A., Heinevetter, L., C^lfen, H., Harding, S. E. Characterization of gliadin-galactomannan incubation mixtures by analytical ultracentrifugation. Part I. Sedimentation velocity. Carbohydr. Polym. 28, 325-332 (1995)

Optima XL-A, sed. equil., M(w); wheat gliadin and locust bean galactomannan; Model E and MOM 3170B analytical ultracentrifuge with schlieren optics, S; gliadin, galactomannan and their interaction; 10 and 15 krpm, 220 and 230 nm (XL-A); PAGE also used; German Institute for Human Nutrition, Arthur-Scheunert-Allee 114-116, D-14558 Bergholz-Rehbrucke, Germany

Proteins: Enzymes

**Artigues, A., Iriarte, A., Martinez-Carrion, M. Acid-induced reversible unfolding of mitochondrial aspartate aminotransferase. J. Biol. Chem. 269, 21990-21999 (1994)

Optima XL-A, sed. vel., S; effect of pH on mammalian mitochondrial aspartate aminotransferase unfolding; An-60 Ti, 6 krpm, 280 nm; CD, fluorescence, PAGE & IR also used; Division of Molecular Biology and Biochemistry, School of Biological Sciences, Univ. of Missouri, Kansas City, MO 64110-2499

**Behal, R. H., DeBuysere, M. S., Demeler, B., Hansen, J. C., Olson, M. S. Pyruvate dehydrogenase multienzyme complex. Characterization of assembly intermediates by sedimentation velocity analysis. J. Biol. Chem. 269, 31372-31377 (1994)

Optima XL-A, sed. vel., S distribution; beef heart pyruvate dehydrogenase multienzyme complex E2-X subcomplex (dissociated and reassociated); 10, 15, 20, 30 & 40 krpm; 280 nm; GuHCl; sucrose gradient centrifugation and PAGE also used; Dept. of Biochemistry, Univ. of Texas Health Science Center, San Antonio, TX 78284-7760

**Birck, C., Vachette, P., Welch, M., Swaren, P., Samama, J.-P. Is the function of the cdc2 kinase subunit proteins tuned by their propensities to oligomerize? Conformational states in solution of the cdc2 kinase partners p13(suc1) and p9(cksphy). Biochemistry 35, 5577-5585 (1996)

Optima XL-A, sed. equil., sed. vel., M(r), f, S, v-bar; Physarum polycephalum and Schizosaccharomyces pombe cdc2 kinase subunit proteins; An-60 Ti, 35 krpm (s.e.), 65 krpm (s.v.), 278 nm, 20deg.C; mass spectrometry, SEC and X-ray scattering also used; (Samama) Groupe de Cristallographie Biologique du Laboratoire de Pharmacologie et de Toxicologie Fondamentales du CNRS, 205 route de Narbonne, 31077 Toulouse, France UPR 8221

**Black, S. D., Martin, S. T. Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3). Biochemistry 33, 12056-12062 (1994)

Optima XL-A, sed. equil., M, degree of association; sed. vel., D, S; Bacillus megaterium cytochrome P450 102; An-60 Ti, 7400-90,700 g (av) (s.v.), 2817 & 5009 g (s.e.), 278 or 418 nm; SEC also used; Dept. of Biochem., Univ. of Texas Health Center at Tyler, Tyler, TX 75710-2003

**Bonnete, F., Ebel, C., Zaccal, G., Elsenberg, H. Biophysical study of halophilic malate dehydrogenase in solution: revised subunit structure and solvent interactions of native and recombinant enzyme. J. Chem. Soc. Faraday Trans. 89, 2659-2666 (1995)

Optima XL-A, sed. equil., m; sed. vel., D, S; native and denatured recombinant malate dehydrogenase; 8, 15 & 30 krpm, 20deg.C, effect of salt concentration; light scattering and densimetry also used; (Zaccal) Inst. de Biologie Structurale, 41 avenue des Martyrs, F-38087 Grenoble Cedex 1, France

**Cann,