G. Marius Clore

Last updated
G. Marius Clore
MAE FRSC FMedSci FRS
Photo of Dr. G. Marius Clore.jpg
Born
Gideon Marius Clore

London, U.K.
Citizenship British, American
Education University 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
Father Leon Clore
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
Fields Molecular Biophysics, Nuclear Magnetic Resonance, Structural Biology, Chemistry
Institutions
Doctoral advisor Sir Arnold Burgen FRS
Notable students
Website gmclore.org/clore

G. Marius Clore MAE, FRSC, FMedSci, FRS is a British-born, Anglo-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 Fellow of the Academy of Medical Sciences, a Fellow of the American Academy of Arts and Sciences, 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]

Contents

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 Academy of Medical Sciences, 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 550 published scientific articles and an h-index (number of papers cited h or more time) of 144. [39] Clore is also one of only five NIH scientists to have been elected to both the United States National Academy of Sciences and The Royal Society, the other four being Julius Axelrod, Francis Collins, Harold Varmus and Ad Bax.

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

Related Research Articles

Nuclear magnetic resonance spectroscopy of proteins is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.

Xplor-NIH is a highly sophisticated and flexible biomolecular structure determination program which includes an interface to the legacy X-PLOR program. The main developers are Charles Schwieters and Marius Clore of the National Institutes of Health. Xplor-NIH is based on a C++ framework with an extensive Python interface enabling very powerful and easy scripting of complex structure determination and refinement protocols. Restraints derived from all current solution and many solid state nuclear magnetic resonance (NMR) and X-ray scattering experiments can be accommodated during structure calculations. Extensive facilities are also available for many types of ensemble calculations where the experimental data cannot be accounted for by a unique structure. Many of the structure calculation protocols involve the use of simulated annealing designed to overcome local minima on the path of the global minimum region of the target function. These calculations can be carried out using any combination of Cartesian, torsion angle and rigid body dynamics and minimization. Currently Xplor-NIH is the most versatile, comprehensive and widely used structure determination/refinement package in NMR structure determination.

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References

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  19. 1 2 "American Academy of Arts and Sciences Fellows".
  20. 1 2 "Elected Members of Academia Europaea 2015".
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  22. ↑ 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. Bibcode:2000PNAS...97.9021C. doi: 10.1073/pnas.97.16.9021 . PMC   16814 . PMID   10922057.
  23. ↑ 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. Bibcode:1998PNAS...95.5891M. doi: 10.1073/pnas.95.11.5891 . PMC   34492 . PMID   9600889.
  24. 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. doi:10.1016/j.tibs.2013.08.003. PMC   3831880 . PMID   24055245.
  25. ↑ 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. Bibcode:2014PNMRS..80....1S. doi:10.1016/j.pnmrs.2014.03.001. PMC   4057650 . PMID   24924264.
  26. ↑ 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. doi:10.1021/bi00484a006. PMID   2223770.
  27. ↑ 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.
  28. ↑ Anthis NJ, Clore GM (2015). "Visualizing transient dark states by NMR spectroscopy". Quarterly Reviews of Biophysics. 48 (1): 35–116. doi:10.1017/S0033583514000122. PMC   6276111 . PMID   25710841.
  29. ↑ 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. S2CID   4427016.
  30. ↑ 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. S2CID   4422087.
  31. ↑ 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. S2CID   4362128.
  32. ↑ "NMR advance brings proteins into the open". Neurosciencenews.com. 25 June 2013.
  33. ↑ 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.
  34. ↑ Libich DS, Tugarinov V, Clore GM (2015). "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. Bibcode:2015PNAS..112.8817L. doi: 10.1073/pnas.1510083112 . PMC   4517251 . PMID   26124125.
  35. ↑ Kotler SA, Tugarinov V, Schmidt T, Ceccon A, Libich DS, Ghirlando R, Schwieters CD, Clore GM (2019). "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. Bibcode:2019PNAS..116.3562K. doi: 10.1073/pnas.1821216116 . PMC   6397591 . PMID   30808748.
  36. ↑ Ceccon A, Tugarinov V, Ghirlando R, Clore GM (2020). "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. Bibcode:2020PNAS..117.5844C. doi: 10.1073/pnas.1922264117 . PMC   7084121 . PMID   32127471.
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  39. ↑ "Google scholar profile".
  40. ↑ "Academy of Medical Sciences announces new Fellows of 2024".
  41. ↑ "G. Marius Clore 2021 Murray Goodman Memorial Prize Winner".
  42. ↑ "UCL Awards 2021 Honorary Degrees and Fellowships". 15 July 2021.
  43. ↑ "G. Marius Clore 2021 Royal Society of Chemistry Khorana Prize Winner".
  44. ↑ "G. Marius Clore to Receive Biophysical Society 2020 Innovation Award".
  45. ↑ "Biophysical Society September 2019 Press Release".
  46. ↑ "Biochemical Society Award Winners for 2013 - Biochemist e-volution" (PDF). Biochemical Society.
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