Alan Fersht

Early life and education

Fersht was born on 21 April 1943[23] in Hackney, London. He was educated at Sir George Monoux Grammar School, an all-boys grammar school in Walthamstow, London.[23] He went on to study at 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 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 & Caius College and Imperial College.[11]

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.[1]

Selected publications

  • Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding[25]
  • The Selected Papers of Sir Alan Fersht: Development of Protein Engineering[26]

Awards and honours

Fersht was elected a Fellow of the Royal Society (FRS) in 1983.[27] 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,[28] 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 (FMedSci).[6] His nomination for the Royal Society reads:

Distinguished for work on mechanisms of enzyme catalysis, especially by stopped and quenched flow methods. He showed that a slow relaxation of chymotrypsin was not a chemical step on the reaction pathway, but a pH-dependent isomerisation between active and inactive forms, and investigated the energetics and equilibria of the transition. He elucidated the leaving-group specificity, leading to a detailed structural interpretation which showed the energetics of "strain" at the binding site. Another experiment dispelled final doubts about the role of a tetrahedral intermediate. More recently Fersht has studied a more complex group of enzymes, the aminoacyl tRNA synthetases. He demonstrated that their precise specificity depends on consecutive independent recognition steps, and under appropriate conditions he trapped a transiently discharged aminoacyl tRNA. Fersht has shown how binding energy can be used to enhance either specificity or rate in an enzymatic reaction, leading to a demonstration of thermodynamic limitations on mechanisms of the "induced fit" type.[27]

Fersht holds an honorary doctorate from Uppsala University (1999).[29]

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;[30][31] Bader Award of the American Chemical Society; Kaj Ulrik Linderstrøm-Lang Prize and Medal; Bijvoet Medal of the Bijvoet Center for Biomolecular Research of Utrecht University in 2008 and the Gilbert N. Lewis Medal University of California, Berkeley, and the Wilhelm Exner Medal in 2009.[32]

In 2003 he was knighted for his pioneering work on protein science.[23] His citation on elected to the Academy of Medical Sciences reads:

Herchel Smith Professor of Organic Chemistry at the MRC Centre for Protein Engineering, Cambridge, Sir Alan is one of the world's leading protein scientists. He was elected to the Royal Society in his late 30s in 1983 for his work illuminating enzymic catalysis and how enzymes attain high fidelity in the translation of the genetic code. Subsequently he was one of the pioneering founders of protein engineering, developing it as an analytical procedure for understanding interactions in proteins and enzyme catalysis. This radical new approach unravelled the relationships between the structure, activity and function of proteins. The full power of his methods became apparent in his seminal and far reaching contributions to the field of protein folding and stability. These studies opened the way to development of novel therapies in cancer and other diseases. He currently works on mutations that affect the stability and activity of the tumour suppressor p53 and how mutants may be "rescued" by small molecule drugs. His contributions have been widely recognised nationally and internationally by prizes for both chemistry and molecular biology, and by memberships of foreign academies.[6]

Personal life

Fersht's recreations include chess[33] and horology.[23] He married Marilyn Persell in 1966 and has one son and one daughter.[23]


  1. Alan Fersht publications indexed by Google Scholar
  2. Alan Fersht LMB Profile
  3. Clarke, Jane (1993). Studies of disulphide mutants of barnase. (PhD thesis). University of Cambridge. OCLC 53666398. EThOS
  4. "Women at Cambridge: Jane Clarke". University of Cambridge. Archived from the original on 24 March 2015.
  5. Clarke, J; Fersht, A. R. (1993). "Engineered disulfide bonds as probes of the folding pathway of barnase: Increasing the stability of proteins against the rate of denaturation". Biochemistry. 32 (16): 4322–9. doi:10.1021/bi00067a022. PMID 8476861.
  6. "Professor Sir Alan Fersht FRS FMedSci". Academy of Medical Sciences. Archived from the original on 17 April 2015.
  7. "Professor Sir Alan Fersht FRS, Department of Chemistry, University of Cambridge". Retrieved 26 July 2011.
  8. 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.
  9. 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. Bibcode:1985Natur.314..235F. doi:10.1038/314235a0. PMID 3845322.
  10. 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. Bibcode:1989Natur.340..122M. doi:10.1038/340122a0. PMID 2739734.
  11. 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.
  12. 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.
  13. Wilkinson, A. J. (2010). "The Selected Papers of Sir Alan Fersht: Development of Protein Engineering". Protein Engineering Design and Selection. 24 (1–2): 225–227. doi:10.1093/protein/gzq103.
  14. 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 978-1-84816-554-0.
  15. Fersht, Alan (1985). Enzyme structure and mechanism. San Francisco: W.H. Freeman. ISBN 0-7167-1614-3.
  16. "Professor Sir Alan Fersht FRS becomes the 42nd Master of Caius". Archived from the original on 22 April 2015. Retrieved 21 November 2012.
  17. Europabio: profile
  18. BBC: brief Fersht career summary at time of knighthood
  19. "Imperial College London: biographical summary Alan Fersht". Archived from the original on 27 June 2009.
  20. "Fersht webpage at MRC Laboratory of Molecular Biology, Cambridge UK". Archived from the original on 14 September 2014.
  21. Alan Fersht's publications indexed by the Scopus bibliographic database. (subscription required)
  22. Fersht, A. R. (2013). "Profile of Martin Karplus, Michael Levitt, and Arieh Warshel, 2013 nobel laureates in chemistry". Proceedings of the National Academy of Sciences of the United States of America. 110 (49): 19656–7. Bibcode:2013PNAS..11019656F. doi:10.1073/pnas.1320569110. PMC 3856823. PMID 24277833.
  23. Anon (2015). "Fersht, Sir Alan (Roy)". Who's Who. (online Oxford University Press ed.). A & C Black, an imprint of Bloomsbury Publishing plc. doi:10.1093/ww/9780199540884.013.U15668. (subscription or UK public library membership required) (subscription required)
  24. Fersht, Alan Roy (1968). Intramolecular Catalysis of Ester Hydrolysis (PhD thesis). University of Cambridge.(subscription required)
  25. Fersht, Alan (2017). Structure and mechanism in protein science : a guide to enzyme catalysis and protein folding. New Jersey. ISBN 9789813225190. OCLC 986523773.
  26. Fersht, Alan; Wang, Qinghua (2010). The selected papers of Sir Alan Fersht : development of protein engineering. London: Imperial College Press. ISBN 9781848165540. OCLC 646400491.
  27. "EC/1983/09: Fersht, Alan Roy". London: The Royal Society. Archived from the original on 13 May 2014.
  28. "Alan Fersht, University of Cambridge, Election Year: 1993". National Academy of Sciences. Archived from the original on 17 April 2015.
  30. "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. doi:10.1002/anie.200462026. PMID 15484254.
  31. "Alan Fersht. 2001 Stein and Moore Award". Protein Science. 10 (4): 905. 2001. PMID 11345067.
  32. editor, ÖGV. (2015). Wilhelm Exner Medal. Austrian Trade Association. ÖGV. Austria.
  33. Fersht, Alan (2007). Jaques Staunton Chess Sets 1849–1939. Kaissa Publications. ISBN 978-0-9557325-0-8.
Academic offices
Preceded by
Sir Christopher Hum
Master of Gonville and Caius College, Cambridge
Succeeded by
Pippa Rogerson
Preceded by
Noreen Murray
Gabor Medal
Succeeded by
Charles Weissmann
Preceded by
Jean-Marie Lehn
Davy Medal
Succeeded by
Malcolm H. Chisholm
Preceded by
Jim Feast
Royal Medal
With: Sir Philip Cohen and Robert E. M. Hedges
Succeeded by
Chris Dobson
Preceded by
Cyril Hilsum
Succeeded by
Ron Laskey
Preceded by
Tomas Lindahl
Succeeded by
C. N. R. Rao
Preceded by
Zdeněk P. Bažant
Wilhelm Exner Medal
With: Christian Wandrey
Succeeded by
Bertil Andersson
Preceded by
Wolfgang Knoll
Succeeded by
Ada Yonath
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.