Alan Fersht

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Sir Alan Roy Fersht
Alan Fersht.jpg
Born (1943-04-21) April 21, 1943 (age 70)
London
Nationality United Kingdom
Fields chemistry
Institutions MRC Laboratory of Molecular Biology
Imperial College London
University of Cambridge
Alma mater Gonville and Caius College, University of Cambridge
Notable students Sir Greg Winter
Known for protein folding
Notable awards Gabor Medal (1991)
Davy Medal (1998)
Royal Medal (2008)

Sir Alan Roy Fersht, FRS (born 21 April 1943) is a British chemist at the MRC Laboratory of Molecular Biology in Cambridge.[1] He is distinguished for his pioneering work on protein folding.[2][3][4][5][6][7][8] Since October 2012, he has been Master of Gonville and Caius College, Cambridge.[9]

Biography[edit]

Alan Fersht was educated at Sir George Monoux Grammar School in Walthamstow, London and at the University of Cambridge, where he was awarded his PhD degree in 1968.

He was Wolfson Research Professor of the Royal Society and Professor of Biological Chemistry at Imperial College London from 1978 to 1988 and was Herchel Smith Professor of Organic Chemistry at Cambridge from 1988 to 2010. He was the Director of the Cambridge Centre for Protein Engineering from 1990 to 2010. He is a Fellow of both Gonville and Caius College and Imperial College.

Alan Fersht is widely regarded as one of the main pioneers of protein engineering, which he developed as a primary method for analysis of the structure, activity and folding of proteins. He has developed methods for the high resolution of protein folding in the sub-millisecond time-scale and has pioneered the method of phi value analysis for studying the folding transition states of proteins. His interests also include protein misfolding, disease and cancer.

He was elected a Fellow of the Royal Society in 1983, by whom he was awarded the Gabor Medal in 1991 for molecular biology, in 1998 the Davy Medal for chemistry and in 2008 the Royal Medal. He is a Foreign Associate of the United States National Academy of Sciences, a Foreign Member of the American Philosophical Society, a Foreign Member of the Accademia dei Lincei, an Honorary Foreign Member of the American Academy of Arts and Sciences and a Fellow of the Academy of Medical Sciences.

He has honorary doctorates from: Uppsala University; Free University of Brussels; Weizmann Institute of Science; Hebrew University of Jerusalem; and University of Aarhus.

He has received many prizes and medals including: the FEBS Anniversary Prize; Novo Biotechnology Award; Charmian Medal of the Royal Society of Chemistry; Max Tishler Lecture and Prize Harvard University; The Datta Lectureship and Medal of the Federation of European Biochemical Societies; Jubilee Lecture and the Harden Medal of the Biochemical Society; Feldberg Foundation Prize, Distinguished Service Award, Miami Nature Biotechnology Winter Symposium; Christian B. Anfinsen Award of the Protein Society; Natural Products Award of the Royal Society of Chemistry, Stein and Moore Award of the Protein Society; Bader Award of the American Chemical Society; Kaj Ulrik Linderstrøm-Lang Prize and Medal; Johannes Martin Bijvoet Medal Utrecht University; and the Gilbert N. Lewis Medal University of California, Berkeley.

In 2003 he was knighted for his pioneering work on protein science.

References[edit]

  1. ^ "Professor Sir Alan Fersht FRS, Department of Chemistry, University of Cambridge". Retrieved 2011-07-26. 
  2. ^ Jackson, S. E.; Fersht, A. R. (1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition". Biochemistry 30 (43): 10428–10435. doi:10.1021/bi00107a010. PMID 1931967.  edit
  3. ^ Fersht, A. R.; Shi, J. P.; Knill-Jones, J.; Lowe, D. M.; Wilkinson, A. J.; Blow, D. M.; Brick, P.; Carter, P.; Waye, M. M. Y.; Winter, G. (1985). "Hydrogen bonding and biological specificity analysed by protein engineering". Nature 314 (6008): 235–238. doi:10.1038/314235a0. PMID 3845322.  edit
  4. ^ Matouschek, A.; Kellis, J. T.; Serrano, L.; Fersht, A. R. (1989). "Mapping the transition state and pathway of protein folding by protein engineering". Nature 340 (6229): 122–126. doi:10.1038/340122a0. PMID 2739734.  edit
  5. ^ Fersht, A.; Matouschek, A.; Serrano, L. (1992). "The folding of an enzyme I. Theory of protein engineering analysis of stability and pathway of protein folding". Journal of Molecular Biology 224 (3): 771–782. doi:10.1016/0022-2836(92)90561-W. PMID 1569556.  edit
  6. ^ Fersht, Alan (1999). Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. San Francisco: W.H. Freeman. ISBN 0-7167-3268-8. 
  7. ^ Qinghua Wang; Fersht, Alan (2010). Selected Papers of Sir Alan Fersht: The Development of Protein Engineering (Icp Selected Papers). River Edge, N.J: Imperial College Press. ISBN 1-84816-554-4. 
  8. ^ Fersht, Alan (1985). Enzyme structure and mechanism. San Francisco: W.H. Freeman. ISBN 0-7167-1614-3. 
  9. ^ "Professor Sir Alan Fersht FRS becomes the 42nd Master of Caius". Retrieved 2012-11-21. 

Further reading[edit]

  • Fersht, Alan (2007). Jaques Staunton Chess Sets 1849-1939. Kaissa Publications. ISBN 0-9557325-0-6. 

External links[edit]

Academic offices
Preceded by
Sir Christopher Hum
Master of Gonville and Caius College,
University of Cambridge

2012-present
Succeeded by
incumbent