G. Marius Clore, M.D., Ph.D.
NIH Distinguished Investigator
Protein Nuclear Magnetic Resonance Section, Laboratory of Chemical Physics
Building 5, Room B130
5 Memorial Drive
Bethesda, MD 20814
The purpose of my lab’s research is to understand the interrelationship between the structure, dynamics, and function of proteins.
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.
- NIH 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
Wälti MA, Libich DS, Clore GM. Extensive Sampling of the Cavity of the GroEL Nanomachine by Protein Substrates Probed by Paramagnetic Relaxation Enhancement. J Phys Chem Lett. 2018;9(12):3368-3371.
Libich DS, Tugarinov V, Clore GM. Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR. Proc Natl Acad Sci U S A. 2015;112(29):8817-23.
Deshmukh L, Louis JM, Ghirlando R, Clore GM. Transient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations. Proc Natl Acad Sci U S A. 2016;113(44):12456-12461.
Deshmukh L, Tugarinov V, Appella DH, Clore GM. Targeting a Dark Excited State of HIV-1 Nucleocapsid by Antiretroviral Thioesters Revealed by NMR Spectroscopy. Angew Chem Int Ed Engl. 2018;57(10):2687-2691.
Deshmukh L, Tugarinov V, Louis JM, Clore GM. Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR. Proc Natl Acad Sci U S A. 2017;114(46):E9855-E9862.
Related Scientific Focus Areas
Biomedical Engineering and Biophysics
This page was last updated on September 14th, 2017