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Alan Fersht

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Title: Alan Fersht  
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Subject: Andreas Matouschek, Jane Clarke (scientist), Department of Chemistry, University of Cambridge, List of Masters of Gonville and Caius College, Cambridge, Fellows of Gonville and Caius College, Cambridge
Collection: 1943 Births, Academics of Imperial College London, British Chemists, British Jews, English Biophysicists, Fellows of Gonville and Caius College, Cambridge, Fellows of the Academy of Medical Sciences, Fellows of the Royal Society, Jewish Chemists, Jewish Scientists, Living People, Masters of Gonville and Caius College, Cambridge, Members of the European Molecular Biology Organization, Members of the United States National Academy of Sciences, Members of the University of Cambridge Department of Chemistry, People Educated at Sir George Monoux College, People from Walthamstow, Royal Medal Winners
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Alan Fersht

Sir Alan Fersht
Born Alan Roy Fersht
(1943-04-21) 21 April 1943 [1]
Nationality United Kingdom
Alma mater University of Cambridge
Thesis Intramolecular catalysis of ester hydrolysis (1968)
Doctoral students
Known for Protein folding
Notable awards
Spouse Marilyn Persell (m. 1966)[1]

Sir Alan Roy Fersht, FRS, FMedSci[7] (born 21 April 1943) is a British chemist at the Laboratory of Molecular Biology and an Emeritus Professor in the Department of Chemistry at the University of Cambridge.[8] He is distinguished for his pioneering work on protein folding.[9][10][11][12][13][14][15][16] Since October 2012, he has been Master of Gonville and Caius College, Cambridge.[17][18][19][20][21][22][23]


  • Early life 1
  • Career and research 2
  • Awards and honours 3
  • Personal life 4
  • References 5

Early life

Fersht was born on 21 April 1943.[1] He was educated at all-boys grammar school in Walthamstow, London.[1] He went on to study at the Gonville and Caius College, Cambridge, where he was awarded his PhD degree in 1968.[24]

Career and research

Fersht was Wolfson Research Professor of the Centre for Protein Engineering from 1990 to 2010. He is a Fellow of both Gonville and Caius College and Imperial College.[12]

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 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.[2]

Awards and honours

Fersht's name on Staircase L at Gonville & Caius College, Cambridge in 2010.

Fersht was elected a Fellow of the Royal Society (FRS) in 1983.[6] The Royal Society awarded him 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,[5] 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.[7] His nomination for the Royal Society reads:

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

Fersht 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;[25][26] 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, and the Wilhelm Exner Medal in 2009.[27]

In 2003 he was knighted for his pioneering work on protein science.[1] His citation on elected to the Academy of Medical Sciences reads:

Personal life

Fersht's recreations include chess[28] and horology.[1] He married Marilyn Persell in 1966 and has one son and one daughter.[1]


  1. ^ a b c d e f g FERSHT, Sir Alan (Roy).   (subscription required)
  2. ^ a b Alan Fersht's publications indexed by Google Scholar, a service provided by Google
  3. ^ "Women at Cambridge: Jane Clarke". University of Cambridge. Archived from the original on 2015-03-24. 
  4. ^  
  5. ^ a b "Alan Fersht, University of Cambridge, Election Year: 1993". National Academy of Sciences. Archived from the original on 2015-04-17. 
  6. ^ a b c "EC/1983/09: Fersht, Alan Roy". London: The Royal Society. Archived from the original on 2014-05-13. 
  7. ^ a b c d "Professor Sir Alan Fersht FRS FMedSci". Academy of Medical Sciences. Archived from the original on 2015-04-17. 
  8. ^ "Professor Sir Alan Fersht FRS, Department of Chemistry, University of Cambridge". Retrieved 2011-07-26. 
  9. ^ Jackson, S. E.; Fersht, A. R. (1991). "Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition". Biochemistry 30 (43): 10428–10435.  
  10. ^ 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.  
  11. ^ 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.  
  12. ^ a b 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.  
  13. ^ Fersht, Alan (1999). Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. San Francisco: W.H. Freeman.  
  14. ^ Wilkinson, A. J. (2010). "The Selected Papers of Sir Alan Fersht: Development of Protein Engineering". Protein Engineering Design and Selection 24: 225.  
  15. ^ 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.  
  16. ^ Fersht, Alan (1985). Enzyme structure and mechanism. San Francisco: W.H. Freeman.  
  17. ^ "Professor Sir Alan Fersht FRS becomes the 42nd Master of Caius". Archived from the original on 4 Apr 2015. Retrieved 2012-11-21. 
  18. ^ Europabio: profile
  19. ^ BBC: brief Fersht career summary at time of knighthood
  20. ^ "Imperial College London: biographical summary Alan Fersht". Archived from the original on 2009-06-27. 
  21. ^ "Fersht webpage at MRC Laboratory of Molecular Biology, Cambridge UK". Archived from the original on 2014-09-14. 
  22. ^ Alan Fersht's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
  23. ^ Fersht, A. R. (2013). "Profile of Martin Karplus, Michael Levitt, and Arieh Warshel, 2013 nobel laureates in chemistry".  
  24. ^ Fersht, Alan Roy (1968). Intramolecular catalysis of ester hydrolysis (PhD thesis). University of Cambridge. (subscription required)
  25. ^ "Alan R. Fersht receives Bader Award / Corey Award to David W. C. Mac Millan / Breslow Award to Peter B. Dervan". Angewandte Chemie International Edition 43 (41): 5430. 2004.  
  26. ^ "Alan Fersht. 2001 Stein and Moore Award". Protein science : a publication of the Protein Society 10 (4): 905. 2001.  
  27. ^ Editor, ÖGV. (2015). Wilhelm Exner Medal. Austrian Trade Association. ÖGV. Austria.
  28. ^ Fersht, Alan (2007). Jaques Staunton Chess Sets 1849-1939. Kaissa Publications.  
Academic offices
Preceded by
Sir Christopher Hum
Master of Gonville and Caius College,
University of Cambridge

Succeeded by

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