Marius Clore is a 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’s work which revealed new insights into macromolecular recognition, 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.
Clore is an elected Member of the United States National Academy of Sciences, and a Fellow of the American Academy of Arts and Sciences. Prizes include the Royal Society of Chemistry Centenary Prize, and the Biochemical Society Centenary Award.
NIH Distinguished Investigator and Chief of the Section of Structural and Molecular Biophysics, Laboratory of Chemical Physics, National Institutes of Health (NIH) NIH Distinguished Investigator and Chief of the Section of Molecular and Structural Biophysics, Laboratory of Chemical Physics, National Institutes of Health (NIH)