Alan Fersht

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Sir Alan Fersht
Alan Fersht.jpg
Born Alan Roy Fersht
(1943-04-21) 21 April 1943 (age 80)[1]
London
Nationality United Kingdom
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Alma mater University of Cambridge
Thesis Intramolecular catalysis of ester hydrolysis (1968)
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Known for Protein folding
Notable awards <templatestyles src="Plainlist/styles.css"/>
Spouse Marilyn Persell (m. 1966)[1]
Website
www.ch.cam.ac.uk/person/arf25

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

Fersht was born on 21 April 1943.[1] He was educated at Sir George Monoux Grammar School, an 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 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.[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:

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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: <templatestyles src="Template:Blockquote/styles.css" />

Herchel Smith Professor of Organic Chemistry at the MRC Centre for Protein Engineering, Cambridge, Sir Alan is the of the world’s leading protein scientists. He was elected to the Royal Society in his late 30’s 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.[7]

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]

References

  1. 1.0 1.1 1.2 1.3 1.4 1.5 1.6 Lua error in package.lua at line 80: module 'strict' not found. (subscription required)
  2. 2.0 2.1 Alan Fersht's publications indexed by Google Scholar, a service provided by Google
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  18. Europabio: profile[dead link]
  19. BBC: brief Fersht career summary at time of knighthood
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  22. Alan Fersht's publications indexed by the Scopus bibliographic database, a service provided by Elsevier.
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  27. Editor, ÖGV. (2015). Wilhelm Exner Medal. Austrian Trade Association. ÖGV. Austria.
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Academic offices
Preceded by Master of Gonville and Caius College,
University of Cambridge

2012-present
Succeeded by
incumbent