Position

Senior Research Associate Boston Biomedical Research Institute

Education

B.A. Hunter College, New York, NY Chemisrty, 1985

Ph.D University of California, Berkeley, CA, Comparative Biochemistry, 1992

Research Interests

Protein Folding, Stability and Function

Selected Publications

Goldberg, J.M. & R.L. Baldwin (1999) A specific transition state for the combination of unfolded S-peptide and folded S-protein, and subsequent refolding. Proc. Nat. Acad. Sci. USA, (in press).

Kim, D. E., Yi, Q., Gladwin, S.T., Goldberg, J.M. & D. Baker (1998) The single helix in protein L is disrupted at the rate limiting step in folding. J. Mol. Biol. 284, 807-815

Goldberg, J.M., & R.L.Baldwin, (1998) Kinetic mechanism of a partial folding reaction. 2. Nature of the trasition state. Biochemistry, 37, 2556-2563

Goldberg, J.M., & R.L. Baldwin, (1998) Kinetic mechanism of a partial folding reaction. 1. Properties of the reaction and effects of denaturants. Biochemistry, 37, 2546-2555.

Goldberg, J.M., & J.F. Kirsch (1996) The reaction catalyzed by Escherichia coli aspartate aminotransferase has multiple partially rate-determining steps, while that catalyzed by the Y225F mutant is dominated by ketimine hydrosis. Biochemistry, 35, 5280-5291

Deng, H., Goldberg, J.M., Kirsch, J.F., & R. Callender (1993) Elucidation of the solution strucure of the Escherichia coli aspartate aminotransferase- methyl-L-aspartate complex by isotope-edited Raman difference spectroscopy. J.Am. Chem. Soc. 115,8869-8870.

Goldberg, J.M., Zheng, J., Deng, H., Chen, Y. Q., Callender, R., & J. Kirsch F. (1993) Structure of the complex between pyridoxal 5'-phosphate and tyrosine 225-to phenylalanine mutant of Escherichia coli aspartate aminotransferase determined by isotope-edited clasical Raman difference spectroscopy. Biochemistry, 32, 8092-8097.

Goldberg, J.M., Swanson, R.V., Goodman, H.S., & J.F. Kirsch, (1991) The Tyr-225-to-Phe mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both Kcat and Km. Biochemistry 30, 305-312.

Kirsch, J.F., Toney, M.D. & J.M.Goldberg (1990) Chemical rescue and change in rate determining step elicited by site directed mutagenesis probes of aspartate aminotransferase. Protein and Pharmaceutical Engineering, Wiley-Liss inc., New York, 105-108

Rice, G.A. Touchette, N.A., Creager, A. N. H., Goldberg, J.M. & R.D. Cole (1998) A high melting strucure in DNA distinguishes phases of the cell cycle. Experimental Cell Research 177, 221-226.

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