Thursday, January 5, 2012 - 11:00am
Dr. Dimitar Pachov, HHMI Research Associate, Kern’s Group, Brandeis University, MA
Due to their dynamic nature relevant to biological activity, biomolecules frequently interconvert between functional substates. Determining how these visits to different conformational states are physically characterized remains a challenging task. We employ computational strategies in conjunction with NMR experiments to reveal – in atomistic resolution – features of transition states and molecular mechanisms along conformational pathways of the signaling protein Nitrogen Regulatory Protein C (NtrC) and the enzyme Adenylate Kinase (Adk).
