Biography:G. Marius Clore

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Short description: Molecular biophysicist, structural biologist
G. Marius Clore

MAE FRSC FRS
Marius Clore Royal Society.jpg
Born
Gideon Marius Clore

(1955-06-06) 6 June 1955 (age 68)
London, U.K.
CitizenshipBritish, American
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 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)
•Royal Society of Chemistry Khorana Prize (2021)
Scientific career
FieldsMolecular Biophysics, Nuclear Magnetic Resonance, Structural Biology, Chemistry
Institutions
  • MRC National Institute for Medical Research, London.
  • Max Planck Institute of Biochemistry, Martinsried, Germany.
  • National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, U.S.
Doctoral advisorSir Arnold Burgen FRS
Notable students
  • Robert T. Clubb
  • Hartmut Oschkinat
  • Julie Forman-Kay FRS
Websitegmclore.org

G. Marius Clore MAE, FRSC, FRS is a British-born, American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual U.S./U.K. Citizen.[1][2][3] He is a Member of the National Academy of Sciences,[4] a Fellow of the Royal Society,[5] a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics 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] Clore's discovery of previously undetectable, functionally significant, rare transient states of macromolecules has yielded fundamental new insights into the mechanisms of important biological processes, and in particular the significance of weak interactions and the mechanisms whereby the opposing constraints of speed and specificity are optimized. Further, Clore's work opens up a new era of pharmacology and drug design as it is now possible to target structures and conformations that have been heretofore unseen.[13]

Biography

Clore received his undergraduate degree with first class honours in biochemistry from University College London in 1976 and medical degree from UCL 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 joint Lister Institute Research Fellowship from the Lister Institute of Preventive Medicine which he held from 1982 to 1984 at the Medical Research Council.[14] In 1984 he joined the Max Planck Institute for Biochemistry in Martinsried, Germany, where he headed the Biological NMR department 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., 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.[15] He has remained at the NIH ever since and is currently a NIH Distinguished Investigator and Chief of the Section on Molecular and Structural Biophysics at the NIH.[4] He is an elected Member of the United States National Academy of Sciences,[16] a Fellow of the Royal Society,[17] a Fellow of the American Academy of Arts and Sciences,[18][19] and a Foreign Member of the Academia Europaea (Biochemistry and Molecular Biology Section).[20] Clore's citation upon election to the Royal Society reads:

"Clore pioneered the development of NMR for determining three-dimensional structures of biological macromolecules and has consistently extended the frontiers of NMR to ever more complex systems. His work on the development of paramagnetic and other relaxation-based NMR experiments to detect and visualize transient, rare states of macromolecules, invisible to conventional structural and biophysical techniques, has shed unique insights into how macromolecules efficiently locate their binding partners, provided the first atomic view of the dynamic amyloid Aß assembly process from disordered peptides into protofibrils, and directly demonstrated that the apo state of the chaperonin GroEL possesses intrinsic foldase/unfoldase activities."[5]

Research

3D structure determination in solution by NMR

Clore played a pivotal role in the development of three- and four-dimensional NMR spectroscopy,[21] the use of residual dipolar couplings for structure determination,[22] the development of simulated annealing and restrained molecular dynamics for three-dimensional protein and nucleic acid structure determination,[23] the solution NMR structure determination of large protein complexes,[24] the development of the combined use of NMR and small-angle X-ray scattering in solution structure determination,[25] and the analysis and characterization of protein dynamics by NMR.[26] 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.[24] Clore is also one of the main authors of the very widely used XPLOR-NIH NMR structure determination program[27]

Detection and visualization of excited and sparsely-populated states

Clore's 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 detect, characterize and visualize the structure and dynamics of sparsely-populated states of macromolecules, which are important in macromolecular interactions but invisible to conventional structural and biophysical techniques.[28] Examples of 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;[29] the detection, visualization and characterization of encounter complexes in protein-protein association;[30] the analysis of the synergistic effects of conformational selection and induced fit in protein-ligand interactions;[31] 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.[32] The latter includes an atomic-resolution view of the dynamics of the amyloid-β aggregation process.[33] and the demonstration of intrinsic unfoldase/foldase activity of the macromolecular machine GroEL.[34] These various techniques have also been used to uncover the kinetic pathway of pre-nucleation transient oligomerization events and associated structures involving the protein encoded by huntingtin exon-1, which may provide a potential avenue for therapeutic intervention in Huntington's disease, a fatal autosomal dominant, neurodegenerative condition.[35][36]

Scientific impact

Clore is one of the most highly cited scientists in the fields of molecular biophysics, structural biology, biomolecular NMR and chemistry[37][38] with over 540 published scientific articles and an h-index (number of papers cited h or more time) of 142.[39] Clore is also one of only four NIH scientists to have been elected to both the United States National Academy of Sciences and The Royal Society, the other three being Julius Axelrod, Francis Collins and Harold Varmus.

Personal life

Marius Clore was educated at the Lycee Francais Charles de Gaulle in Kensington, London, University College London and UCL Medical School. Marius Clore's father was the film producer Leon Clore whose credits include The French Lieutenant's Woman.

Awards and honors

References

  1. ↑ 1.0 1.1 "Profile of Marius Clore". Proceedings of the National Academy of Sciences of the United States of America 113 (45): 12604–12606. 2016. doi:10.1073/pnas.1616528113. PMID 27799541. Bibcode: 2016PNAS..11312604S. 
  2. ↑ 2.0 2.1 Clore, G. Marius. "Curriculum Vitae". https://spin.niddk.nih.gov/clore/CV/Clore_Complete_CV_Biblio_April2020.pdf. 
  3. ↑ "American Institute of Physics Oral History Interviews - Marius Clore interviewed by David Zierler". 24 June 2020. https://www.aip.org/history-programs/niels-bohr-library/oral-histories/44402. 
  4. ↑ 4.0 4.1 4.2 4.3 "G. Marius Clore". National Academy of Sciences. http://www.nasonline.org/member-directory/members/20033168.html. 
  5. ↑ 5.0 5.1 5.2 "G. Marius Clore". Royal Society. https://royalsociety.org/people/G-Marius-Clore-25341/. 
  6. ↑ "G. Marius Clore, MD, Ph.D., NIH Distinguished Investigator". https://irp.nih.gov/pi/g-marius-clore. 
  7. ↑ "G. Marius Clore, MD, Ph.D., FRS, NIH Distinguished Investigator". https://www.niddk.nih.gov/about-niddk/staff-directory/biography/c/clore-marius. 
  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. doi:10.1038/332303a0. PMID 3352729. Bibcode: 1988Natur.332..303R. 
  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. ↑ "Cell biology: brief encounters bolster contacts". Nature 444 (7117): 279–280. 2006. doi:10.1038/nature05306. PMID 17051147. Bibcode: 2006Natur.444..279B. 
  12. ↑ "Clore named Royal Society Fellow". https://www.asbmb.org/asbmb-today/people/060120/clore-named-royal-society-fellow-remembering-paul. 
  13. ↑ "Targeting a dark excited state of HIV-1 nucleocapsid by anti-retroviral thioesters revealed by NMR spectroscopy". Angewandte Chemie International Edition 57 (10): 2687–2691. 2018. doi:10.1002/anie.201713172. PMID 29345807. 
  14. ↑ 14.0 14.1 "Former Fellows of the Lister Institute of Preventive Medicine". https://www.lister-institute.org.uk/former-fellows/. 
  15. ↑ Clore, Marius G (2011). "Adventures in Biomolecular NMR". in Harris, Robin K; Wasylishen, Roderick L. Encyclopedia of Magnetic Resonance. John Wiley & Sons. doi:10.1002/9780470034590. ISBN 978-0-470-03459-0. http://spin.niddk.nih.gov/clore/Pub/pdf/432.pdf. 
  16. ↑ "2014 Press release of National Academy of Sciences Members and Foreign Associates Elected". http://www.nasonline.org/news-and-multimedia/news/april-29-2014-NAS-Election.html. 
  17. ↑ "2020 Royal Society press release of outstanding scientists elected as Fellows and Foreign Members". https://royalsociety.org/news/2020/04/outstanding-scientists-elected-as-fellows-and-foreign-members-of-the-royal-society/. 
  18. ↑ 18.0 18.1 "Book of Members, 1780-2014: Chapter B". American Academy of Arts and Sciences. https://www.amacad.org/multimedia/pdfs/publications/bookofmembers/ChapterC.pdf. 
  19. ↑ 19.0 19.1 "American Academy of Arts and Sciences Fellows". https://members.amacad.org/G.Clore. 
  20. ↑ 20.0 20.1 "Elected Members of Academia Europaea 2015". http://www.ae-info.org/ae/Acad_Main/News/Elected%20members%202015. 
  21. ↑ "Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy". Science 252 (5011): 1390–1399. 1991. doi:10.1126/science.2047852. PMID 2047852. Bibcode: 1991Sci...252.1390M. 
  22. ↑ "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. 2000. doi:10.1073/pnas.97.16.9021. PMID 10922057. Bibcode: 2000PNAS...97.9021C. 
  23. ↑ "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. 1998. doi:10.1073/pnas.95.11.5891. PMID 9600889. Bibcode: 1998PNAS...95.5891M. 
  24. ↑ 24.0 24.1 "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. 2013. doi:10.1016/j.tibs.2013.08.003. PMID 24055245. 
  25. ↑ "Using small angle solution scattering data in Xplor-NIH structure calculations.". Progress in Nuclear Magnetic Resonance Spectroscopy 80: 1–11. 2014. doi:10.1016/j.pnmrs.2014.03.001. PMID 24924264. 
  26. ↑ "Analysis of backbone dynamics of interleukin-1beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy". Biochemistry 29 (32): 7387–7401. 1990. doi:10.1021/bi00484a006. PMID 2223770. 
  27. ↑ "The Xplor-NIH NMR molecular structure determination package". Journal of Magnetic Resonance 160 (1): 65–73. 2003. doi:10.1016/S1090-7807(02)00014-9. PMID 12565051. Bibcode: 2003JMagR.160...65S. https://zenodo.org/record/1260200. 
  28. ↑ "Visualizing transient dark states by NMR spectroscopy". Quarterly Reviews of Biophysics 48 (1): 35–116. 2015. doi:10.1017/S0033583514000122. PMID 25710841. 
  29. ↑ "Detecting transient intermediates in macromolecular binding by paramagnetic NMR". Nature 440 (7088): 1227–1230. 2006. doi:10.1038/nature04673. PMID 16642002. Bibcode: 2006Natur.440.1227I. 
  30. ↑ "Visualization of transient encounter complexes in protein-protein association". Nature 444 (7117): 383–386. 2006. doi:10.1038/nature05201. PMID 17051159. Bibcode: 2006Natur.444..383T. 
  31. ↑ "Open-to-closed transition in apo-maltose-binding protein visualized by paramagnetic NMR". Nature 449 (7165): 1078–1082. 2007. doi:10.1038/nature06232. PMID 17960247. Bibcode: 2007Natur.449.1078T. 
  32. ↑ "NMR advance brings proteins into the open". Neurosciencenews.com. 25 June 2013. http://neurosciencenews.com/neuroimaging-groel-beta-amyloid-electrophysiology-258/. 
  33. ↑ "Atomic resolution dynamics on the surface of amyloid beta protofibrils probed by solution NMR". Nature 480 (7376): 268–272. 2011. doi:10.1038/nature10577. PMID 22037310. Bibcode: 2011Natur.480..268F. 
  34. ↑ "Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR". Proc. Natl. Acad. Sci. U.S.A. 112 (29): 8817–8823. 2015. doi:10.1073/pnas.1510083112. PMID 26124125. Bibcode: 2015PNAS..112.8817L. 
  35. ↑ "probing the initial transient oligomerization events facilitating Huntingtin fibril nucleation at atomic resolution by relaxation-based NMR". Proc. Natl. Acad. Sci. U.S.A. 116 (9): 3562–3571. 2019. doi:10.1073/pnas.1821216116. PMID 30808748. Bibcode: 2019PNAS..116.3562K. 
  36. ↑ "Abrogation of prenucleation, transient oligomerization of the huntingtin exon-1 protein by human profilin". Proc. Natl. Acad. Sci. U.S.A. 117 (11): 5844–5852. 2020. doi:10.1073/pnas.1922264117. PMID 32127471. Bibcode: 2020PNAS..117.5844C. 
  37. ↑ "Top 10 researchers in chemistry based on total citations". Times Higher Education. 9 October 2008. http://www.timeshighereducation.co.uk/news/top-10-researchers-in-chemistry-based-on-total-citations/403915.article. 
  38. ↑ "Royal Society of Chemistry h-index ranking of living chemists". http://diyhpl.us/~bryan/papers2/H-index%20ranking%20of%20living%20chemists%20%28April%202010%29.pdf. 
  39. ↑ "Google scholar profile". https://scholar.google.com/citations?user=5KmWmkEAAAAJ&hl=en. 
  40. ↑ "G. Marius Clore 2021 Murray Goodman Memorial Prize Winner". https://onlinelibrary.wiley.com/page/journal/10970282/homepage/murray_goodman_memorial_prize.htm. 
  41. ↑ "UCL Awards 2021 Honorary Degrees and Fellowships". 15 July 2021. https://www.ucl.ac.uk/news/2021/jul/ucl-awards-2021-honorary-degrees-and-fellowships. 
  42. ↑ "G. Marius Clore 2021 Royal Society of Chemistry Khorana Prize Winner". https://www.rsc.org/prizes-funding/prizes/2021-winners/dr-g-marius-clore/. 
  43. ↑ "G. Marius Clore to Receive Biophysical Society 2020 Innovation Award". https://www.biophysics.org/news-room/g-marius-clore-to-receive-2020-innovation-award. 
  44. ↑ "Biophysical Society September 2019 Press Release". https://www.biophysics.org/news-room/acat/1/archive/9-2019. 
  45. ↑ "Biochemical Society Award Winners for 2013 - Biochemist e-volution". Biochemical Society. http://www.biochemist.org/bio/03403/0060/034030060.pdf. 
  46. ↑ "The Centenary Award". biochemistry.org. http://www.biochemistry.org/Awards/TheCentenaryAward.aspx. 
  47. ↑ "Centenary Prize Winner 2011". rsc.org. http://www.rsc.org/ScienceAndTechnology/Awards/CentenaryPrizes/2011winnerclore.asp. 
  48. ↑ "List of elected ISMAR fellows". https://wws.weizmann.ac.il/ISMAR/ismar-organization#ismar-fellows/. 
  49. ↑ Chemical Society of Washington Hillebrand Award
  50. ↑ "American Society of Biochemistry and Molecular Biology Today, May 2011, ASBMB member update p. 6". http://www.asbmb.org/uploadedFiles/ASBMBToday/Content/Archive/Archived%20Issue%20052011.pdf. 
  51. ↑ "Fellow of the Biophysical Society Award". biophysics.org. http://www.biophysics.org/AwardsFunding/SocietyAwards/FellowoftheBiophysicalSocietyAward/tabid/501/Default.aspx. 
  52. ↑ "Members/Former Fellows". lister-institute.org.uk. http://www.lister-institute.org.uk/fellows/members/. 
  53. ↑ "Fellows of the American Associastion for the Advancement of Science". https://www.aaas.org/fellows/listing. 
  54. ↑ "Protein Society Young Investigator Award". http://www.proteinsociety.org/protein-society-awards/young-investigator-award/. 
  55. ↑ "NIDDK scientists share award". The NIH Record (1993) volume 45(17), page 12. http://nihrecord.nih.gov/PDF_Archive/1993%20PDFs/19930817.pdf. 

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