G. Marius Clore

Last updated
G. Marius Clore

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

London, U.K.
Citizenship British, American
Alma mater 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
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

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]

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 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 143. [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

Related Research Articles

<span class="mw-page-title-main">Structural biology</span> Study of molecular structures in biology

Structural biology, as defined by the Journal of Structural Biology, deals with structural analysis of living material at every level of organization. Early structural biologists throughout the 19th and early 20th centuries were primarily only able to study structures to the limit of the naked eye's visual acuity and through magnifying glasses and light microscopes.

<span class="mw-page-title-main">Spin label</span>

A spin label (SL) is an organic molecule which possesses an unpaired electron, usually on a nitrogen atom, and the ability to bind to another molecule. Spin labels are normally used as tools for probing proteins or biological membrane-local dynamics using electron paramagnetic resonance spectroscopy. The site-directed spin labeling (SDSL) technique allows one to monitor a specific region within a protein. In protein structure examinations, amino acid-specific SLs can be used.

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.

<span class="mw-page-title-main">Frederic M. Richards</span> American biochemist and biophysicist (1925–2009)

Frederic Middlebrook Richards, commonly referred to as Fred Richards, was an American biochemist and biophysicist known for solving the pioneering crystal structure of the ribonuclease S enzyme in 1967 and for defining the concept of solvent-accessible surface. He contributed many key experimental and theoretical results and developed new methods, garnering over 20,000 journal citations in several quite distinct research areas. In addition to the protein crystallography and biochemistry of ribonuclease S, these included solvent accessibility and internal packing of proteins, the first side-chain rotamer library, high-pressure crystallography, new types of chemical tags such as biotin/avidin, the nuclear magnetic resonance (NMR) chemical shift index, and structural and biophysical characterization of the effects of mutations.

<span class="mw-page-title-main">Residual dipolar coupling</span>

The residual dipolar coupling between two spins in a molecule occurs if the molecules in solution exhibit a partial alignment leading to an incomplete averaging of spatially anisotropic dipolar couplings.

Adriaan "Ad" Bax is a Dutch-American molecular biophysicist. He was born in the Netherlands and is the Chief of the Section on Biophysical NMR Spectroscopy at the National Institutes of Health. He is known for his work on the methodology of biomolecular NMR spectroscopy.

David S. Cafiso is an American biochemist and a professor of chemistry at the University of Virginia. His research focuses on membrane proteins and cell signaling, and is primarily supported by grants from the National Institute of Health.

<span class="mw-page-title-main">Jane S. Richardson</span> American biophysicist

Jane Shelby Richardson is an American biophysicist best known for developing the Richardson diagram, or ribbon diagram, a method of representing the 3D structure of proteins. Ribbon diagrams have become a standard representation of protein structures that has facilitated further investigation of protein structure and function globally. With interests in astronomy, math, physics, botany, and philosophy, Richardson took an unconventional route to establishing a science career. Richardson is a professor in biochemistry at Duke University.

Axel T. Brunger is a German American biophysicist. He is Professor of Molecular and Cellular Physiology at Stanford University, and a Howard Hughes Medical Institute Investigator. He served as the Chair of the Department of Molecular and Cellular Physiology (2013–2017).

<span class="mw-page-title-main">Macromolecular assembly</span>

The term macromolecular assembly (MA) refers to massive chemical structures such as viruses and non-biologic nanoparticles, cellular organelles and membranes and ribosomes, etc. that are complex mixtures of polypeptide, polynucleotide, polysaccharide or other polymeric macromolecules. They are generally of more than one of these types, and the mixtures are defined spatially, and with regard to their underlying chemical composition and structure. Macromolecules are found in living and nonliving things, and are composed of many hundreds or thousands of atoms held together by covalent bonds; they are often characterized by repeating units. Assemblies of these can likewise be biologic or non-biologic, though the MA term is more commonly applied in biology, and the term supramolecular assembly is more often applied in non-biologic contexts. MAs of macromolecules are held in their defined forms by non-covalent intermolecular interactions, and can be in either non-repeating structures, or in repeating linear, circular, spiral, or other patterns. The process by which MAs are formed has been termed molecular self-assembly, a term especially applied in non-biologic contexts. A wide variety of physical/biophysical, chemical/biochemical, and computational methods exist for the study of MA; given the scale of MAs, efforts to elaborate their composition and structure and discern mechanisms underlying their functions are at the forefront of modern structure science.

Dennis Torchia is an American biophysicist who specialized in NMR spectroscopy. He spent most of his career at the National Institute of Dental and Craniofacial Research (NIDCR), part of the United States National Institutes of Health, where he served as Chief of the Structural Biology Unit before his retirement in 2006.

Juli Feigon is a Distinguished Professor of Biochemistry at the University of California, Los Angeles, where she has been a faculty member since 1985. She was elected to the United States National Academy of Sciences in 2009. Her research focuses on structural studies of nucleic acids by nuclear magnetic resonance spectroscopy along with other biophysical techniques.

<span class="mw-page-title-main">Hartmut Oschkinat</span> German structural biologist and professor

Hartmut Oschkinat is a German structural biologist and professor for chemistry at the Free University of Berlin. His research focuses on the study of biological systems with solid-state nuclear magnetic resonance.

Dinshaw J. Patel is an Indian-American structural biologist who holds the Abby Rockefeller Mauzé Chair in Experimental Therapeutics at Memorial Sloan Kettering Cancer Center in New York City.

<span class="mw-page-title-main">William Eaton (scientist)</span> American biophysicist

William Allen Eaton is a biophysical chemist who is a NIH Distinguished Investigator, Chief of the Section on Biophysical Chemistry, and Chief of the Laboratory of Chemical Physics at the National Institute of Diabetes and Digestive and Kidney Diseases, one of the 20 Institutes of the United States National Institutes of Health.

<span class="mw-page-title-main">Mei Hong (chemist)</span> Chinese-American chemist

Mei Hong is a Chinese-American biophysical chemist and professor of chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.

Protein quinary structure refers to the features of protein surfaces that are shaped by evolutionary adaptation to the physiological context of living cells. Quinary structure is thus the fifth level of protein complexity, additional to protein primary, secondary, tertiary and quaternary structures. As opposed to the first four levels of protein structure, which are relevant to isolated proteins in dilute conditions, quinary structure emerges from the crowdedness of the cellular context, in which transient encounters among macromolecules are constantly occurring.

<span class="mw-page-title-main">Alfred G. Redfield</span> American molecular biologist, physicist

Alfred G. Redfield was an American physicist and biochemist. In 1955 he published the Redfield relaxation theory, effectively moving the practice of NMR or Nuclear magnetic resonance from the realm of classical physics to the realm of semiclassical physics. He continued to find novel magnetic resonance applications to solve real-world problems throughout his life.

Bonnie Ann Wallace, FRSC is a British and American biophysicist and biochemist. She is a professor of molecular biophysics in the department of biological sciences, formerly the department of crystallography, at Birkbeck College, University of London, U.K.

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. Bibcode:2016PNAS..11312604S. doi: 10.1073/pnas.1616528113 . PMC   5111653 . PMID   27799541.
  2. 1 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. 24 June 2020. Retrieved 26 June 2020.
  4. 1 2 3 4 "G. Marius Clore". Member Directory. National Academy of Sciences. Retrieved 12 March 2015.
  5. 1 2 3 "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. S2CID   32312775.
  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. S2CID   12357797.
  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. S2CID   4397989.
  12. ↑ "Clore named Royal Society Fellow" . Retrieved 1 June 2020.
  13. ↑ Deshmukh, L, Tugarinov V, Appella DH, Clore GM (2018). "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. doi:10.1002/anie.201713172. PMC   6034507 . PMID   29345807.
  14. 1 2 "Former Fellows of the Lister Institute of Preventive Medicine" . Retrieved 27 June 2020.
  15. ↑ 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   978-0-470-03459-0.
  16. ↑ "2014 Press release of National Academy of Sciences Members and Foreign Associates Elected". Archived from the original on 2015-08-18.
  17. ↑ "2020 Royal Society press release of outstanding scientists elected as Fellows and Foreign Members".
  18. 1 2 "Book of Members, 1780-2014: Chapter B" (PDF). American Academy of Arts and Sciences.
  19. 1 2 "American Academy of Arts and Sciences Fellows".
  20. 1 2 "Elected Members of Academia Europaea 2015".
  21. ↑ Clore GM, Gronenborn AM (1991). "Structures of larger proteins in solution: three- and four-dimensional heteronuclear NMR spectroscopy". Science. 252 (5011): 1390–1399. Bibcode:1991Sci...252.1390M. doi:10.1126/science.2047852. OSTI   83376. PMID   2047852.
  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. 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.
  37. ↑ "Top 10 researchers in chemistry based on total citations". Times Higher Education. 9 October 2008.
  38. ↑ "Royal Society of Chemistry h-index ranking of living chemists" (PDF).
  39. ↑ "Google scholar profile".
  40. ↑ "G. Marius Clore 2021 Murray Goodman Memorial Prize Winner".
  41. ↑ "UCL Awards 2021 Honorary Degrees and Fellowships". 15 July 2021.
  42. ↑ "G. Marius Clore 2021 Royal Society of Chemistry Khorana Prize Winner".
  43. ↑ "G. Marius Clore to Receive Biophysical Society 2020 Innovation Award".
  44. ↑ "Biophysical Society September 2019 Press Release".
  45. ↑ "Biochemical Society Award Winners for 2013 - Biochemist e-volution" (PDF). Biochemical Society.
  46. ↑ "The Centenary Award". biochemistry.org.
  47. ↑ "Centenary Prize Winner 2011". rsc.org.
  48. ↑ "List of elected ISMAR fellows". Archived from the original on 2015-10-27.
  49. ↑ Chemical Society of Washington Hillebrand Award
  50. ↑ "American Society of Biochemistry and Molecular Biology Today, May 2011, ASBMB member update p. 6" (PDF).
  51. ↑ "Fellow of the Biophysical Society Award". biophysics.org.
  52. ↑ "Members/Former Fellows". lister-institute.org.uk. Archived from the original on 2015-08-05. Retrieved 2015-02-19.
  53. ↑ "Fellows of the American Associastion for the Advancement of Science".
  54. ↑ "Protein Society Young Investigator Award". Archived from the original on 2015-02-14. Retrieved 2015-02-19.
  55. ↑ "NIDDK scientists share award" (PDF). The NIH Record (1993) volume 45(17), page 12.
This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.