Tertiary Structural Characterization of Proteins & Protein Complexes

Mass Spectrometry Group

The underlying hypothesis of structural biology is that biophysical characterization of proteins and the interactions of proteins in complexes will provide insight into how proteins fulfill their function. Thus, tertiary structural information of proteins and their specific surfaces involved in interactions with other proteins or DNA are thought to be critical for our understanding of disease mechanisms. Thus, the central research program of the Mass Spectrometry Group has been to develop and apply mass spectrometry-based techniques to determine the molecular recognition sites in protein complexes. Current studies within this major heading include:

• Characterization of antigen proteins related to Sjogren’s Disease and their sites of interaction
• Development and application of surface oxidation of proteins by hydroxyl radicals to the characterization of proteins and protein:protein interactions
• Determination of epitopes, especially those recognized by neutralizing antibodies, recognized by anti-HIV antibodies (partially in collaboration with Dr. Susan Zolla-Pazner, NYU/NY Veterans Hospital)
• Determination of sites of interaction in protein complexes involved in DNA repair (collaborations with the Kunkel and Wilson labs, LSB)
• Determination of discontinuous epitopes on the hepatitis C glycoprotein E2 recognized by neutralizing anti-HCV antibodies (in collaboration with Dr. Steven Foung, Stanford University)
• Determination of epitopes on B. anthracis protective antigen recognized by enhancing monoclonal antibodies (in collaboration with Stephen Little, USAMRIID)
• Characterization of protein:protein interactions involved in competency in bacillus (in collaboration with Prof. John Cavanagh, NCSU)