The Sundberg laboratory is primarily focused on the biophysical analysis and identification of protein-protein interactions, including those that we perturb by mutagenesis techniques in order to derive a fundamental understanding about the nature of how proteins recognize each other specifically, as well as protein complexes that play key roles in disease pathogenesis. Our main experimental tools include:

(1) Surface plasmon resonance (SPR, or Biacore) and isothermal titration calorimetry (ITC) analysis for the derivation of the kinetic and thermodynamic parameters of molecular interactions;

2. (2)X-ray crystallography to determine atomic resolution structures of proteins and protein complexes;
   

3. (3)Directed evolution by phage and yeast display mutagenesis techniques to evolve the affinity of protein-protein complexes for dissecting molecular recognition and therapeutic development;
   

4. (4)Two-hybrid assays, such as the split-ubiquitin assay, to identify novel protein-protein interaction partners;
   

5. (5)tandem mass spectrometry (LC-MS/MS) for the identification of proteins and post-translational modifications involved in biomedically-relevant cellular signaling events.
   

BBRI houses state-of-the art instrumentation for all of our analytical needs, as part of our Core Facilities.

For more details about current projects in the lab, click on the following links:

HIV Immune Evasion: molecular basis of peptide- and allele-specific MHC class I myelomonocytic MHC receptor interactions

HIV Protection: Molecular mechanisms of antibody-dependent cellular cytotoxicity (ADCC)-mediated protection from HIV infection and progression to AIDS

Superantigens: molecular basis of disease and development of novel therapeutics to counteract toxic shock syndrome

Molecular Recognition: quantifying energetic cooperativity and the contributions to binding from disordered protein regions in protein-protein interactions