G. Marius Clore
National Institutes of Health
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Primary Section: 29, Biophysics and Computational Biology Secondary Section: 14, Chemistry Membership Type:
Member
(elected 2014)
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Biosketch
Marius Clore FRS is a Distinguished Investigator in the Laboratory of Chemical Physics at the NIH. He is a molecular biophysicist known for pioneering three-dimensional structure determination of proteins, nucleic acids and their complexes by solution nuclear magnetic resonance (NMR) spectroscopy, and for developing NMR methods for characterizing the structure and dynamics of rare, short-lived conformational states. Clore was born in London, U.K. in 1955 and became a U.S. citizen in 1996. He received his undergraduate degree in Biochemistry from University College London, his medical degree from University College Hospital Medical School, London, and his doctorate from the MRC National Institute for Medical Research in London. He joined the scientific staff of the MRC National Institute for Medical Research in 1980, became head of the biological NMR group at the Max-Planck Institute for Biochemistry (Martinsried, Germany) in 1984, and moved to the NIH in 1988. Awards include: Membership of the National Academy of Sciences; Fellowship of the Royal Society, the Royal Society of Chemistry and the American Academy of Arts and Sciences; the Royal Society of Chemistry Centenary Prize; and the Biochemical Society Centenary Award.
Research Interests
Clore's work which revealed new insights into macromolecular recognition, conformational transitions, and assembly processes, relies on the amplification and transfer, via exchange phenomena, of NMR properties of the invisible sparsely-populated "dark" state(s) onto observable (major) visible species. Examples include how transcription factors locate their specific DNA binding site within a sea of non-specific DNA; the role of encounter complexes in protein-protein association; the interplay of conformational selection and induced fit in protein-ligand interactions; transient interactions of intrinsically disordered and partially folded polypeptides with large megadalton macromolecular assemblies; and the characterization of pre-nucleation, transient oligomerization of huntingtin prior to fibril formation.
