He was Wolfson Research Professor of the Royal Society and Professor of Biological Chemistry at Imperial College London from 1978 to 1988 and is now Herchel Smith Professor of Organic Chemistry at Cambridge. He is the Director of the Cambridge Centre for Protein Engineering (UK).
He is a Fellow of Gonville and Caius College, Cambridge, and also of Imperial College.
Alan Fersht was a pioneer 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, an Honorary Foreign Member of the American Academy of Arts and Sciences and a Fellow of the Academy of Medical Sciences.
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; Datta Lecture and Medal FEBS; Jubilee Lecture and the Harden Medal of the Biochemical Society; Feldberg Foundation Prize, Distinguished Service Award, Miami Nature (journal) 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 folding.