G. Marius Clore

G. Marius Clore FRSC, FRS (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][3] He is a member of the United States National Academy of Sciences,[4] a Fellow of the Royal Society,[5] 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 U.S. National Institutes of Health.[6][7] He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy,[8] for advancing experimental approaches to the study of large macromolecules and their complexes by NMR,[9] and for developing NMR-based methods to study rare conformational states in protein-nucleic acid[10] and protein-protein[11] recognition.[12]

G. Marius Clore

FRSC FRS
Born
Gideon Marius Clore

(1955-06-06) June 6, 1955
London, U.K.
NationalityBritish
CitizenshipUnited States and U.K.
Alma materUniversity College London and University College Hospital Medical School, London, U.K.
Known forLaying 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
Awards•Member of the United States National Academy of Sciences
•Fellow of the Royal Society
•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)
Scientific career
FieldsMolecular Biophysics, Nuclear Magnetic Resonance, Structural Biology
Institutions
Doctoral advisorSir Arnold Burgen FRS
Notable students
Influences
Influenced
Websitespin.niddk.nih.gov/clore

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.[4] 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.[13] 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, U.S.A., 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.[14] He has remained at the NIH ever since and is currently a NIH Distinguished Investigator and Chief of the Section on Protein NMR Spectroscopy at the NIH.[4] He is an elected Member of the United States National Academy of Sciences,[15] a Fellow of the Royal Society,[16] a Fellow of the American Academy of Arts and Sciences,[17][18] and a Foreign Member of the Academia Europaea (Biochemistry and Molecular Biology Section).[19]

Research

He is one of the main authors of the very widely used XPLOR-NIH NMR structure determination program,[20] which evolved from the program X-PLOR developed by Axel Brunger[21] 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.[22]

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.[23] 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;[24] the detection, visualization and characterization of encounter complexes in protein-protein association;[25] the analysis of the synergistic effects of conformational selection and induced fit in protein-ligand interactions;[26] 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.[27] The latter includes an atomic-resolution view of the dynamics of the amyloid-β aggregation process.[28]

Clore is one of the most highly cited scientists in the fields of molecular biophysics, structural biology, biomolecular NMR and chemistry[29][30] with over 500 published scientific articles and an h-index (number of papers cited h or more time) of 135.[31]

Awards

References
  1. Samoray C (2016). "Profile of Marius Clore". Proceedings of the National Academy of Sciences of the United States of America. 113 (45): 12604–12606. doi:10.1073/pnas.1616528113. PMC 5111653. PMID 27799541.CS1 maint: uses authors parameter (link)
  2. Clore, G. Marius. "Curriculum Vitae" (PDF). NIDDK. Retrieved 26 June 2020.
  3. "American Institute of Physics Oral History Interviews - Marius Clore interviewed by David Zierler". AIP. Retrieved 26 June 2020.
  4. "G. Marius Clore". Member Directory. National Academy of Sciences. Retrieved 12 March 2015.
  5. "G. Marius Clore". Member Directory. Royal Society. Retrieved 29 April 2020.
  6. "G. Marius Clore, MD, Ph.D., NIH Distinguished Investigator". National Institutes of Health Intramural Research Program. Retrieved 14 August 2018.
  7. "G. Marius Clore, MD, Ph.D., FRS, NIH Distinguished Investigator". National Institute of Diabetes and Digestive and Kidney Diseases. Retrieved 14 August 2018.
  8. "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 (26): 6598. 2014. doi:10.1002/anie.201405510.
  9. Ringe D (1988). "Protein structure: an extra dimension to NMR". Nature. 332 (6162): 303. Bibcode:1988Natur.332..303R. doi:10.1038/332303a0. PMID 3352729.
  10. Dahlquist FW (2006). "Slip sliding away: new insights into DNA-protein recognition". Nature Chemical Biology. 2 (7): 353–354. doi:10.1038/nchembio0706-353. PMID 16783338.
  11. Blundell TL, Fernandez-Recio J (2006). "Cell biology: brief encounters bolster contacts". Nature. 444 (7117): 279–280. Bibcode:2006Natur.444..279B. doi:10.1038/nature05306. PMID 17051147.CS1 maint: uses authors parameter (link)
  12. "Clore named Royal Society Fellow". Retrieved 1 June 2020.
  13. "Former Fellows of the Lister Institute of Preventive Medicine". Retrieved 27 June 2020.
  14. Clore, Marius G. (2011). "Adventures in Biomolecular NMR" (PDF). In Harris, Robin K; Wasylishen, Roderick L (eds.). Encyclopedia of Magnetic Resonance. John Wiley & Sons. doi:10.1002/9780470034590. hdl:11693/53364. ISBN 9780470034590.
  15. "2014 Press release of National Academy of Sciences Members and Foreign Associates Elected". Archived from the original on 2015-08-18.
  16. "2020 Royal society press release of outstanding scientists elected as Fellows and Foreign Members".
  17. "Book of Members, 1780-2014: Chapter B" (PDF). American Academy of Arts and Sciences.
  18. "American Academy of Arts and Sciences Fellows".
  19. "Elected Members of Academia Europaea 2015".
  20. 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. Bibcode:2003JMagR.160...65S. doi:10.1016/S1090-7807(02)00014-9. PMID 12565051.CS1 maint: uses authors parameter (link)
  21. Güntert, Peter (2011). "Automated protein structure determination from NMR data". In Dingley, Andrew J.; Pascal, Steven M. (eds.). Biomolecular NMR spectroscopy. Advances in Biomedical Spectroscopy. 3. Amsterdam: IOS Press. p. 341. doi:10.3233/978-1-60750-695-9-338. ISBN 9781607506942.
  22. 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. doi:10.1016/j.tibs.2013.08.003. PMC 3831880. PMID 24055245.CS1 maint: uses authors parameter (link)
  23. Anthis NJ, Clore GM (2015). "Visualizing transient dark states by NMR spectroscopy". Quarterly Reviews in Biophysics. 48 (1): 35–116. doi:10.1017/S0033583514000122. PMC 6276111. PMID 25710841.CS1 maint: uses authors parameter (link)
  24. Iwahara J, Clore GM (2006). "Detecting transient intermediates in macromolecular binding by paramagnetic NMR". Nature. 440 (7088): 1227–1230. Bibcode:2006Natur.440.1227I. doi:10.1038/nature04673. PMID 16642002.CS1 maint: uses authors parameter (link)
  25. Tang C, Iwahara J, Clore GM (2006). "Visualization of transient encounter complexes in protein-protein association". Nature. 444 (7117): 383–386. Bibcode:2006Natur.444..383T. doi:10.1038/nature05201. PMID 17051159.CS1 maint: uses authors parameter (link)
  26. 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. Bibcode:2007Natur.449.1078T. doi:10.1038/nature06232. PMID 17960247.CS1 maint: uses authors parameter (link)
  27. "NMR advance brings proteins into the open". Neurosciencenews.com.
  28. 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. Bibcode:2011Natur.480..268F. doi:10.1038/nature10577. PMC 3237923. PMID 22037310.CS1 maint: uses authors parameter (link)
  29. "Top 10 researchers in chemistry based on total citations". Times Higher Education.
  30. "Royal Society of Chemistry h-index ranking of living chemists" (PDF).
  31. "Google scholar profile".
  32. "G. Marius Clore to Receive Biophysical Society 2020 Innovation Award".
  33. "Biophysical Society September 2019 Press Release".
  34. "Biochemical Society Award Winners for 2013 - Biochemist e-volution" (PDF). Biochemical Society.
  35. "The Centenary Award". biochemistry.org.
  36. "Centenary Prize Winner 2011". rsc.org.
  37. "List of elected ISMAR fellows". Archived from the original on 2015-10-27.
  38. Chemical Society of Washington Hillebrand Award
  39. "American Society of Biochemistry and Molecular Biology Today, May 2011, ASBMB member update p. 6" (PDF).
  40. "Fellow of the Biophysical Society Award". biophysics.org.
  41. "Members/Former Fellows". lister-institute.org.uk. Archived from the original on 2015-08-05. Retrieved 2015-02-19.
  42. Thomson Reuters. "Highly Cited Researchers". highlycited.com. Archived from the original on 2015-02-14.
  43. "Fellows of the American Associastion for the Advancement of Science".
  44. "Protein Society Young Investigator Award". Archived from the original on 2015-02-14. Retrieved 2015-02-19.
  45. "NIDDK scientists share award" (PDF). The NIH Record (1993) volume 45(17), page 12.
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