G. Marius Clore

NIH Distinguished Investigator and Chief of the Section of Molecular and Structural Biophysics, Laboratory of Chemical Physics. Member of the National Academy of Sciences, Fellow of the Royal Society and Fellow of the U.K. Academy of Medical Sciences. Developer of nuclear magnetic resonance (NMR) spectroscopy for studying proteins and their complexes in solution, whose experimental and computational approaches have been universally adopted. Recent discovery of paramagnetic relaxation enhancement and dark state exchange saturation transfer to detect and visualize low population intermediates in macromolecular association represents a paradigm shift in understanding macromolecular interactions and sheds new light on highly dynamic processes. Examples include the search for specific binding sites by transcription factors diffusing along DNA,  the formation of transient encounter complexes in weak protein-protein association, analysis of synergistic effects of conformational selection and induced fit in protein-ligand interactions, atomic-resolution view of the dynamics of amyloid-beta aggregation, interaction of protein substrates with the chaperonin GroEL, and demonstration of intrinsic foldase/unfoldase activity of GroEL.