Carol V. Robinson

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Dame Carol Robinson
Born Carol Vivien Bradley
(1956-04-10) 10 April 1956 (age 62)[1]
Nationality UK
Alma mater
Scientific career
Thesis Structural studies on bioactive organic compounds (1982)

Dame Carol Vivien Robinson, DBE FRS FMedSci[8] (née Bradley, born 10 April 1956[1]) is a British chemist. She is a Royal Society Research Professor at the Physical and Theoretical Chemistry Laboratory at the University of Oxford, as well as the Dr Lee's Professor of Chemistry Elect. She was previously Professor of Mass Spectrometry at the Department of Chemistry of the University of Cambridge.[7][9][10][11][12]

Early life and education

Born in Kent, the daughter of Denis E. Bradley and Lillian (née Holder),[13] Carol Vivien Bradley left school at 16 and began her career as a lab technician in Sandwich, Kent with Pfizer, where she began working with the then novel technique of mass spectrometry.[14][citation needed]

Her potential was spotted, and she gained further qualifications at evening classes and day release from her job at Pfizer. After earning her degree, she left Pfizer and studied for a Master of Science degree at the University of Swansea, followed by a PhD at the University of Cambridge,[15] which she completed in just two years, rather than the more usual three.[9] During this time she was a student at Churchill College, Cambridge.[1]

Career and research

After a postdoctoral training fellowship at the University of Bristol,[16] she took up a junior position in the mass spectrometry unit at the University of Oxford, where she began analysing protein folding.[17]Her research on the three-dimensional structure of proteins in particular has demonstrated the power of such techniques in studying large molecular compounds.[18] Much of her research has involved pushing the limits of electrospray mass spectrometry, demonstrating that important complexes can be generated and studied in the gas phase. In addition to her contributions to the study of protein folding, Carol has conducted important work on ribosomes, molecular chaperones and most recently membrane proteins.In 2001, she returned to Cambridge to take up a professorship in the Department of Chemistry, becoming this department's first female professor. She took up her current position in Oxford in 2009.[19][20][21][22][23]

Awards and honours

Robinson was awarded the American Society for Mass Spectrometry's Biemann Medal in 2003, and the Christian B. Anfinsen Award in 2008. In 2004 the Royal Society awarded her both a Fellowship (FRS)[8] and the Rosalind Franklin Award.[24] Her nomination for the Royal Society reads:[8]

Distinguished for her research on the application of mass spectrometry to problems in chemical biology. She has used mass spectrometry to define the folding and binding of interacting proteins in large complexes. Most importantly, she has established that macromolecular complexes such as GroEL, ribosomes, and intact virus capsids can be generated in the gas phase and their electrospray mass spectra recorded. This work has demonstrated the power of mass spectrometry in studying very large complexes and allowed her to define changes in their conformation and the manner of their assembly.

In 2010 Robinson received the Davy Medal "for her ground-breaking and novel use of mass spectrometry for the characterisation of large protein complexes".[25][26]. In 2011 she was given the Interdisciplinary Prize by the Royal Society of Chemistry for "development of a new area of research, gas-phase structural biology, using highly refined mass spectrometry techniques",[27] and the Aston Medal. She has been awarded honorary doctorates from the University of Kent, the University of York, and the University of Bristol.[28]

She was appointed Dame Commander of the Order of the British Empire (DBE) in the 2013 New Year Honours for services to science and industry.[29]

In 2015 she was L'Oréal-UNESCO Awards for Women in Science; "For her groundbreaking work in macromolecular mass spectrometry and pioneering gas phase structural biology by probing the structure and reactivity of single proteins and protein complexes, including membrane proteins."[30]

In 2017 she was elected a Foreign Associate of the US National Academy of Sciences.[31]


  1. ^ a b c d Anon (2015) ROBINSON, Dame Carol Vivien. Who's Who. A & C Black, an imprint of Bloomsbury Publishing plc. closed access publication – behind paywall doi:10.1093/ww/9780199540884.013.U4000698 (subscription required)
  2. ^ Tan, X; Calderon-Villalobos, L. I.; Sharon, M; Zheng, C; Robinson, C. V.; Estelle, M; Zheng, N (2007). "Mechanism of auxin perception by the TIR1 ubiquitin ligase". Nature. 446 (7136): 640–5. Bibcode:2007Natur.446..640T. doi:10.1038/nature05731. PMID 17410169.
  3. ^ Booth, D. R.; Sunde, M; Bellotti, V; Robinson, C. V.; Hutchinson, W. L.; Fraser, P. E.; Hawkins, P. N.; Dobson, C. M.; Radford, S. E.; Blake, C. C.; Pepys, M. B. (1997). "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis". Nature. 385 (6619): 787–93. Bibcode:1997Natur.385..787B. doi:10.1038/385787a0. PMID 9039909.
  4. ^ Jiménez, J. L.; Nettleton, E. J.; Bouchard, M; Robinson, C. V.; Dobson, C. M.; Saibil, H. R. (2002). "The protofilament structure of insulin amyloid fibrils". Proceedings of the National Academy of Sciences of the United States of America. 99 (14): 9196–201. Bibcode:2002PNAS...99.9196J. doi:10.1073/pnas.142459399. PMC 123117. PMID 12093917.
  5. ^ Pepys, M. B.; Hirschfield, G. M.; Tennent, G. A.; Gallimore, J.; Kahan, M. C.; Bellotti, V.; Hawkins, P. N.; Myers, R. M.; Smith, M. D.; Polara, A.; Cobb, A. J. A.; Ley, S. V.; Aquilina, J.; Robinson, C. V.; Sharif, I.; Gray, G. A.; Sabin, C. A.; Jenvey, M. C.; Kolstoe, S. E.; Thompson, D.; Wood, S. P. (2006). "Targeting C-reactive protein for the treatment of cardiovascular disease". Nature. 440 (7088): 1217–1221. Bibcode:2006Natur.440.1217P. doi:10.1038/nature04672. PMID 16642000.
  6. ^ Miranker, A; Robinson, C. V.; Radford, S. E.; Aplin, R. T.; Dobson, C. M. (1993). "Detection of transient protein folding populations by mass spectrometry". Science. 262 (5135): 896–900. Bibcode:1993Sci...262..896M. doi:10.1126/science.8235611. PMID 8235611.
  7. ^ a b Pain, Elisabeth (2011). "An Interview with Carol Robinson". Science. doi:10.1126/science.caredit.a1100023.
  8. ^ a b c Anon (2004). "EC/2004/37: Robinson, Carol Vivien". London: Royal Society. Archived from the original on 23 July 2014.
  9. ^ a b Al-Khalili, Jim (2014). "Carol Robinson interviewed on The Life Scientific". BBC.
  10. ^ Robinson, C. V. (2011). "Women in science: In pursuit of female chemists". Nature. 476 (7360): 273–5. Bibcode:2011Natur.476..273R. doi:10.1038/476273a. PMID 21850083.
  11. ^ Carol V. Robinson publications indexed by the Scopus bibliographic database. (subscription required)
  12. ^ Carol Robinson's Official website
  13. ^ "Births June 1956: Index entry". FreeBMD. ONS. Retrieved 23 July 2014.
  14. ^ Sullivan, Ruth (12 December 2014). "Dame Carol Robinson: from school leaver at 16 to leading chemist". Financial Times. ISSN 0307-1766. Retrieved 5 August 2016.
  15. ^ Bradley, Carol Vivien (1982). Structural studies on bioactive organic compounds. (PhD thesis). University of Cambridge. EThOS
  16. ^ "Professor Dame Carol Robinson, FRS, Doctor of Science, 15 July 2013". University of Bristol. Archived from the original on 18 November 2014.
  17. ^ Crace, John (22 June 2004). "Carol Robinson: Society doyenne". The Guardian. Archived from the original on 2 March 2014.
  18. ^ "Carol Robinson". Retrieved 2017-11-24.
  19. ^ "Carol Robinson Profile". University of Oxford. Archived from the original on 5 March 2014.
  20. ^ Hall, Z; Hernández, H; Marsh, J. A.; Teichmann, S. A.; Robinson, C. V. (2013). "The role of salt bridges, charge density, and subunit flexibility in determining disassembly routes of protein complexes". Structure. 21 (8): 1325–37. doi:10.1016/j.str.2013.06.004. PMC 3737473. PMID 23850452.
  21. ^ Marsh, J. A.; Hernández, H; Hall, Z; Ahnert, S. E.; Perica, T; Robinson, C. V.; Teichmann, S. A. (2013). "Protein complexes are under evolutionary selection to assemble via ordered pathways". Cell. 153 (2): 461–70. doi:10.1016/j.cell.2013.02.044. PMC 4009401. PMID 23582331.
  22. ^ Levy, E. D.; Boeri Erba, E; Robinson, C. V.; Teichmann, S. A. (2008). "Assembly reflects evolution of protein complexes". Nature. 453 (7199): 1262–5. Bibcode:2008Natur.453.1262L. doi:10.1038/nature06942. PMC 2658002. PMID 18563089.
  23. ^ Ruotolo, B. T. (2005). "Evidence for Macromolecular Protein Rings in the Absence of Bulk Water". Science. 310 (5754): 1658. Bibcode:2005Sci...310.1658R. doi:10.1126/science.1120177. PMID 16293722.
  24. ^ "Finding the right balance: from rare gases to ribosomes". Archived from the original on 10 August 2014.
  25. ^ "The Davy Medal (1877)". The Royal Society. Archived from the original on 16 March 2015.
  26. ^ Loo, J. A.; Gross, M. L. (2004). "Focus in honor of Carol V. Robinson, 2003 Biemann Medal awardee". Journal of the American Society for Mass Spectrometry. 15 (10): 1379. doi:10.1016/j.jasms.2004.07.011.
  27. ^ "Interdisciplinary Prize 2011 Winner".
  28. ^ "Carol Robinson awards". University of Oxford. Archived from the original on 5 March 2014.
  29. ^ Anon (2012) "No. 60367". The London Gazette (Supplement). 29 December 2012. p. 7.
  30. ^ 2015 L'Oréal-UNESCO For Women in Science Awards, Arnold Nou, 2 April 2015, Retrieved 4 April 2015
  31. ^ "News from the National Academy of Sciences". National Academy of Sciences. 2 May 2017. Retrieved 3 May 2017.

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