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G. Marius Clore, M.D., Ph.D., NIH Distinguished Investigator

Photo of Marius Clore
Scientific Focus Areas: Biomedical Engineering and Biophysics, Structural Biology

Professional Experience

  • NIH Distinguished Investigator, NIDDK, NIH (2011-present)
  • NIH Senior Investigator, NIDDK, NIH, 1988-present
  • Head, Biological NMR Group, Max Planck Institute for Biochemistry, Martinsried, Germany, 1984-1988
  • Member of Scientific Staff, MRC National Institute for Medical Research, London, U.K., 1980-1984
  • House Surgeon, St. Charles Hospital (St. Mary's Group), 1980
  • House Physician, University College Hospital, 1979-1980
  • Ph.D., MRC National Institute for Medical Research, London, 1982
  • M.D., University College hospital Medical School  London, 1979
  • B.Sc. (1st class honors), University College, London, 1976

Research Goal

The purpose of my lab’s research is to understand the interrelationship between the structure, dynamics, and function of proteins. A particular focus is the study of rare, highly transient, “excited” states of proteins and their complexes that play a key role of molecular recognition.

Current Research

Our lab studies the structure and dynamics of proteins, protein-protein complexes, and protein-nucleic acid complexes using multidimensional nuclear magnetic resonance (NMR) spectroscopy, and we develop and apply novel NMR and computational methods to aid in these studies.  We are particularly interested in complexes involved in signal transduction and transcriptional regulation, and on AIDS and AIDS-related proteins.  More recently we have focused on the development of novel NMR methods to detect, visualize, and characterize transient, sparsely-populated states of macromolecules.  Such states, which are invisible to conventional biophysical techniques, including crystallography, play a critical role in macromolecular recognition, allostery induced fit, conformational selection, and molecular assembly. Dr. Clore is an elected member of the National Academy of Sciences, the American Academy of Arts and Sciences, and Academia Europaea.

Applying our Research

This research will facilitate targeted and rational drug design.

Select Publications

Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement.
Wälti MA, Libich DS, Clore GM.
J Phys Chem Lett (2018 Jun 21) 9:3368-3371. Abstract/Full Text
Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.
Libich DS, Tugarinov V, Clore GM.
Proc Natl Acad Sci U S A (2015 Jul 21) 112:8817-23. Abstract/Full Text
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Research in Plain Language

Our lab is developing new tools and techniques that facilitate the study of the structure and dynamics of proteins and protein complexes, functional units that include one or more proteins. Our studies rely on nuclear magnetic resonance (NMR) spectroscopy, a research approach that relies on the magnetic properties of the nucleus of certain atoms to determine physical and chemical properties of the molecules in which they are contained.

Currently, we are especially interested in developing novel NMR approaches to detect and visualize short-lived, sparsely-populated states that are invisible to conventional biophysical and structural techniques. Such species play a critical role in recognition and molecular assembly. Other interests include the development of hybrid strategies to solve the structures of large (> 100 kDa) complexes using a combination of NMR and solution X-ray scattering techniques.

Our research extends the use of NMR to studies that were previously impossible. For instance, NMR can be used for larger structures. The many proteins and protein complexes we describe are resulting in new insights into fundamental cell operations. Our many advances in the use of NMR also include the development of mathematical algorithms and computational techniques that are making analysis of NMR data faster and more efficient.

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