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 3. Staff Directory
 4. G. Marius Clore, M.D., Ph.D., FRS, NIH Distinguished Investigator

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G. MARIUS CLORE, M.D., PH.D., FRS, NIH DISTINGUISHED INVESTIGATOR

Section Chief: Section of Molecular and Structural Biophysics, Laboratory of
Chemical Physics
Scientific Focus Areas: Biomedical Engineering and Biophysics, Structural
Biology
mariusc@intra.niddk.nih.gov 301-496-0782 ResearchGate Google Scholar ORCID Add
to Contacts
View My Lab
Biography Pages
 * Overview
 * Publications


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 a Fellow of the
Royal Society, a Member of the National Academy of Sciences, a Fellow of the
American Academy of Arts and Sciences, and a Foreign Member of the Academia
Europaea. Prizes and awards include the Royal Society of Chemistry Centenary and
Khorana Prizes, the Biochemical Society (U.K.) Centenary Award, The Biophysical
Society Innovation Award, and the Biopolymers Murray Goodman Memorial Prize.


APPLYING OUR RESEARCH

This research will facilitate targeted and rational drug design.


SELECT PUBLICATIONS

Nucleation of Huntingtin Aggregation Proceeds via Conformational Conversion of
Pre-Formed, Sparsely-Populated Tetramers. Torricella F, Tugarinov V, Clore GM.
Adv Sci (Weinh) (2024 Jun) 11:e2309217. Abstract/Full Text NIH external link
Time-resolved DEER EPR and solid-state NMR afford kinetic and structural
elucidation of substrate binding to Ca(2+)-ligated calmodulin. Schmidt T, Jeon
J, Yau WM, Schwieters CD, Tycko R, Clore GM. Proc Natl Acad Sci U S A (2022 Feb
8) 119. Abstract/Full Text NIH external link View More Publications


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.


RELATED LINKS

 * Dr. Clore's Curriculum Vitae (PDF, 883 KB)
 * National Academy of Science Profile External link
 * Academia Europaea (The Academy of Europe) Profile External link
 * Wikipedia listing External link
 * Royal Society Profile External link




RESEARCH IMAGES

Partially closed state of apo maltose binding protein

Structures of complexes from the bacterial phosphotransferasesystem

15N Dark-state Exchange Saturation Transfer (DEST) spectroscopy

Last Reviewed April 2024


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