G. Marius Clore

G. Marius Clore
Born (1955-06-06) June 6, 1955
London, U.K.
Residence United States
Citizenship United States and U.K.
Nationality British
Fields Nuclear magnetic resonance, biophysics, structural biology
Institutions National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Alma mater University College London and University College Hospital Medical School
Doctoral advisor Sir Arnold Burgen FRS
Known for Laying the foundations for three-dimensional protein structure determination in solution by NMR, developing innovative approaches for extending NMR to larger and more complex systems, and using NMR to uncover invisible states of proteins
Notable awards •Member of the United States National Academy of Sciences
•Fellow of the American Academy of Arts and Sciences
•Foreign Member of the Academia Europaea
•Royal Society of Chemistry Centenary Prize (2011)
•Biochemical Society Centenary Award (2013]
Website
spin.niddk.nih.gov/clore

G. Marius Clore FRSC (born June 6, 1955) is a British-born American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual US/U.K. Citizen.[1][2] He is a member of the United States National Academy of Sciences,[3] a NIH Distinguished Investigator, and the Chief of the Protein NMR Spectroscopy Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the National Institutes of Health. He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy,[4] for advancing experimental approaches to the study of large macromolecules and their complexes by NMR,[5] and for developing NMR-based methods to study rare conformational states in protein-nucleic acid[6] and protein-protein[7] recognition.

Biography

Clore received his undergraduate degree with first class honours in biochemistry from University College London in 1976 and medical degree from University College Hospital Medical School in 1979.[3] After completing house physician and house surgeon appointments at University College Hospital and St. Charles Hospital (part of the St. Mary's Hospital group), respectively, he was a member of the scientific staff of the Medical Research Council National Institute for Medical Research from 1980 to 1984. He received his PhD from the National Institute for Medical Research in Physical Biochemistry in 1982. He was awarded a Lister Institute Research Fellowship from the Lister Institute for Preventive Medicine which he held from 1982 to 1984 at the Medical Research Council. In 1984 he joined the Max Planck Institute for Biochemistry in Martinsried, Germany, where he headed the Biological NMR group from 1984 to 1988.[1][2]

In 1988, Clore was recruited to the National Institutes of Health (NIH) Laboratory of Chemical Physics (National Institute of Diabetes and Digestive and Kidney Diseases) located in Bethesda, Maryland, where he interacted closely in the late 1980s and early 1990s with NIH colleagues Ad Bax, Angela Gronenborn and Dennis Torchia on the development of multidimensional heteronuclear NMR spectroscopy and a structural biology effort aimed at proteins involved in the pathogenesis of HIV/AIDS.[8] He has remained at the NIH ever since and is currently an NIH Distinguished Investigator and Chief of the Section on Protein NMR Spectroscopy at the NIH.[3] He is an elected Member of the United States National Academy of Sciences,[9] a Fellow of the American Academy of Arts and Sciences,[10] and a Foreign Member of the Academia Europaea (Biochemistry and Molecular Biology Section).[11]

Research

Clore is known for the development of three- and four-dimensional NMR spectroscopy,[12] the use of residual dipolar couplings for structure determination,[13] the development of simulated annealing and restrained molecular dynamics for three-dimensional protein and nucleic acid structure determination,[14] the solution NMR structure determination of large protein complexes,[15] the development of the combined use of NMR and small-angle X-ray scattering in solution structure determination,[16] and the analysis and characterization of protein dynamics by NMR.[17] He is one of the main authors of the very widely used XPLOR-NIH NMR structure determination program,[18] which evolved from the program X-PLOR developed by Axel Brunger[19] and originally based on the program CHARMM-F that ran on Cray supercomputers. Clore's work on complexes of all the cytoplasmic components of the bacterial phosphotransferase system (PTS) led to significant insights into how signal transduction proteins recognize multiple, structurally dissimilar partners by generating similar binding surfaces from completely different structural elements and exploiting side chain conformational plasticity.[15]

His recent work has focused on developing new NMR methods (such as paramagnetic relaxation enhancement, dark state exchange saturation transfer spectroscopy and lifetime line broadening) to characterize the structure and dynamics of sparsely-populated states of macromolecules, which are important in macromolecular interactions but invisible to conventional structural and biophysical techniques.[20] Examples of recent work include the direct demonstration of rotation-coupled sliding and intermolecular translocation as mechanisms whereby sequence-specific DNA binding proteins locate their target site(s) within an overwhelming sea of non-specific DNA sequences;[21] the detection, visualization and characterization of encounter complexes in protein-protein association;[22] the analysis of the synergistic effects of conformational selection and induced fit in protein-ligand interactions;[23] and the uncovering of "dark", spectroscopically invisible states in interactions of NMR-visible proteins and polypeptides (including intrinsically disordered states) with very large megadalton macromolecular assemblies.[24] The latter includes an atomic-resolution view of the dynamics of the amyloid-β aggregation process.[25]

Clore is one of the most highly cited scientists in the fields of molecular biophysics, structural biology, biomolecular NMR and chemistry[26][27] with over 490 published scientific articles and an h-index (number of papers cited h or more time) of 126.[28]

Awards

References

  1. 1 2 Samoray C (2016). "Profile of Marius Clore". Proceedings of the National Academy of Sciences of the United States of America. 113 (45): 12604–12606. PMID 27799541. doi:10.1073/pnas.1616528113.
  2. 1 2 Clore, G. Marius. "Curriculum Vitae" (PDF). NIDDK. Retrieved 16 December 2016.
  3. 1 2 3 4 "G. Marius Clore". Member Directory. National Academy of Sciences. Retrieved 12 March 2015.
  4. ↑ "New Members and Foreign Associates of the National Academy of Sciences: G. Marius Clore, Gregory C. Fu, Sir J. Fraser Stoddart, Ei-ichi Negishi". Angewandte Chemie International Edition. 53: 6598. 2014. doi:10.1002/anie.201405510.
  5. ↑ Ringe D (1988). "Protein structure: an extra dimension to NMR". Nature. 332 (6162): 303. PMID 3352729. doi:10.1038/332303a0.
  6. ↑ Dahlquist FW (2006). "Slip sliding away: new insights into DNA-protein recognition". Nature Chemical Biology. 2: 353–354. PMID 16783338. doi:10.1038/nchembio0706-353.
  7. ↑ Blundell TL, Fernandez-Recio J (2006). "Cell biology: brief encounters bolster contacts". Nature. 444 (7117): 279–280. PMID 17051147. doi:10.1038/nature05306.
  8. ↑ Clore, Marius G. (2011). "Adventures in Biomolecular NMR". Encyclopedia of Magnetic Resonance (PDF). John Wiley & Sons. ISBN 9780470034590. doi:10.1002/9780470034590.
  9. ↑ "2014 Press release of National Academy of Sciences Members and Foreign Associates Elected".
  10. 1 2 "Book of Members, 1780-2014: Chapter B" (PDF). American Academy of Arts and Sciences.
  11. 1 2 "Elected Members of Academia Europaea 2015".
  12. ↑ Clore GM, Gronenborn AM (1991). "Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy". Science. 252 (5011): 1390–1399. PMID 2047852. doi:10.1126/science.2047852.
  13. ↑ Clore GM (2000). "Accurate and rapid docking of protein-protein complexes on the basis of intermolecular nuclear Overhauser enhancement data and dipolar couplings by rigid body minimization". Proceedings of the National Academy of Sciences USA. 97 (16): 9021–9025. PMC 16814 Freely accessible. PMID 10922057. doi:10.1073/pnas.97.16.9021.
  14. ↑ Clore GM, Gronenborn AM (1998). "New methods of structure refinement for macromolecular structure determination by NMR". Proceedings of the National Academy of Sciences of the United States of America. 95 (11): 5891–5898. PMC 34492 Freely accessible. PMID 9600889. doi:10.1073/pnas.95.11.5891.
  15. 1 2 Clore GM, Venditti V (2013). "Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate:sugar phosphotransferase system". Trends in Biochemical Sciences. 38 (10): 515–530. PMC 3831880 Freely accessible. PMID 24055245. doi:10.1016/j.tibs.2013.08.003.
  16. ↑ Schwieters CD, Clore, GM (2014). "Using small angle solution scattering data in Xplor-NIH structure calculations.". Progress in Nuclear Magnetic Resonance Spectroscopy. 80: 1–11. PMC 4057650 Freely accessible. PMID 24924264. doi:10.1016/j.pnmrs.2014.03.001.
  17. ↑ Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM (1990). "Analysis of backbone dynamics of interleukin-1beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy". Biochemistry. 29 (32): 7387–7401. PMID 2223770. doi:10.1021/bi00484a006.
  18. ↑ Schwieters CD, Kuszewski JJ, Tjandra N, Clore GM (2003). "The Xplor-NIH NMR molecular structure determination package". Journal of Magnetic Resonance. 160 (1): 65–73. PMID 12565051. doi:10.1016/S1090-7807(02)00014-9.
  19. ↑ Güntert, Peter (2011). "Automated protein structure determination from NMR data". In Dingley, Andrew J.; Pascal, Steven M. Biomolecular NMR spectroscopy. Amsterdam: IOS Press. p. 341. ISBN 9781607506942. doi:10.3233/978-1-60750-695-9-338.
  20. ↑ Anthis NJ, Clore GM (2015). "Visualizing transient dark states by NMR spectroscopy". Quarterly Reviews in Biophysics. 48 (1): 35–116. PMID 25710841. doi:10.1017/S0033583514000122.
  21. ↑ Iwahara J, Clore GM (2006). "Detecting transient intermediates in macromolecular binding by paramagnetic NMR". Nature. 440 (7088): 1227–1230. PMID 16642002. doi:10.1038/nature04673.
  22. ↑ Tang C, Iwahara J, Clore GM (2006). "Visualization of transient encounter complexes in protein-protein association". Nature. 444 (7117): 383–386. PMID 17051159. doi:10.1038/nature05201.
  23. ↑ Tang C, Schwieters CD, Clore GM (2007). "Open-to-closed transition in apo-maltose-binding protein visualized by paramagnetic NMR". Nature. 449 (7165): 1078–1082. PMID 17960247. doi:10.1038/nature06232.
  24. ↑ "NMR advance brings proteins into the open". Neurosciencenews.com.
  25. ↑ Fawzi NL, Ying J, Ghirlando R, Torchia DA, Clore GM (2011). "Atomic resolution dynamics on the surface of amyloid beta protofibrils probed by solution NMR". Nature. 480 (7376): 268–272. PMC 3237923 Freely accessible. PMID 22037310. doi:10.1038/nature10577.
  26. ↑ "Top 10 researchers in chemistry based on total citations". Times Higher Education.
  27. ↑ "Royal Society of Chemistry h-index ranking of living chemists" (PDF).
  28. ↑ "Google scholar profile".
  29. ↑ "Biochemical Society Award Winners for 2013 - Biochemist e-volution" (PDF). Biochemical Society.
  30. ↑ "The Centenary Award". biochemistry.org.
  31. ↑ "Centenary Prize Winner 2011". rsc.org.
  32. ↑ "List of elected ISMAR fellows". Archived from the original on 2015-10-27.
  33. ↑ Chemical Society of Washington Hillebrand Award
  34. ↑ "American Society of Biochemistry and Molecular Biology Today, May 2011, ASBMB member update p. 6" (PDF).
  35. ↑ "Fellow of the Biophysical Society Award". biophysics.org.
  36. ↑ "Members/Former Fellows". lister-institute.org.uk.
  37. ↑ Thomson Reuters. "Highly Cited Researchers". highlycited.com. Archived from the original on 2015-02-14.
  38. ↑ Fellows of the AAAS
  39. ↑ Protein Society Young Investigator Award
  40. ↑ "NIDDK scientists share award" (PDF). The NIH Record (1993) volume 45(17), page 12.
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