32 Facts About Alan Fersht

Sir Alan Roy Fersht was born on 21 April 1943 and is a British chemist at the MRC Laboratory of Molecular Biology, Cambridge, and an Emeritus Professor in the Department of Chemistry at the University of Cambridge.

Alan Fersht was Master of Gonville and Caius College, Cambridge from 2012 to 2018.

Alan Fersht's father, Philip, was a ladies' tailor and his mother, Betty, a dressmaker.

Alan Fersht's grandparents were Jewish immigrants from Poland, Lithuania and Belarus.

Alan Fersht was a keen chess player and was the Essex County Junior champion in 1961.

Alan Fersht was awarded a State Scholarship to read Natural Sciences at Gonville and Caius College, Cambridge, where he obtained First Class in Pt I of the Natural Sciences Tripos in 1964, First Class in Pt II in 1965 and was awarded his PhD degree in 1968.

Alan Fersht spent a post-doctoral year at Brandeis University working under William Jencks.

Alan Fersht returned to Cambridge in 1969 as a group leader at the MRC Laboratory of Molecular Biology until 1977 and a junior research fellow at Jesus College, Cambridge until 1972.

Alan Fersht was Wolfson Research Professor of the Royal Society and Professor of Biological Chemistry at Imperial College London from 1978 to 1988.

Alan Fersht spent a sabbatical year at Stanford University on an Eleanor Roosevelt Fellowship of the American Cancer Society with Arthur Kornberg.

Alan Fersht was Herchel Smith Professor of Organic Chemistry at Cambridge from 1988 to 2010.

Alan Fersht was the Director of the Cambridge Centre for Protein Engineering from 1990 to 2010 when, on reaching the retirement age, he became an Emeritus Group Leader at the MRC Laboratory of Molecular Biology.

Alan Fersht is a Life Fellow of Gonville and Caius College.

Alan Fersht studied for his PhD intramolecular catalysis in the hydrolysis of aspirin as a model for catalysis by enzymes.

Alan Fersht was recruited by David Mervyn Blow and Max Perutz at the MRC Laboratory of Molecular Biology to work on the mechanism of the enzymes that were being solved there.

Alan Fersht pointed out that of Michaelis-Menten kinetics is the parameter that measures the capacity of an enzyme to discriminate between substrates that are available simultaneously, and so it provides the only meaningful physiological definition of specificity.

Alan Fersht used measurements of to quantify the role of binding energies in catalysis and specificity, particularly in the fidelity of selection of amino acids during protein biosynthesis by the aminoacyl-tRNA synthetases, where he formulated the double-sieve editing mechanism.

Alan Fersht was one of the first classical enzymologists to use Recombinant DNA technology, which he learned in the laboratory of Arthur Kornberg, while measuring the fidelity of DNA replication from kinetics of mutagenesis in vivo.

Alan Fersht went on to pioneer protein engineering as a tool for analysing protein structure and mechanism while Winter as a tool for antibody engineering.

Alan Fersht showed that Free-energy relationships can be applied to analyse non-covalent interactions in transition states of enzyme-catalysed reactions and infer their structures in an analogous procedure to physical chemical methods for transition states in covalent reactions by measuring changes in the kinetics and thermodynamics on small changes in the structure of reagents.

Alan Fersht was elected a Fellow of the Royal Society in 1983.

Alan Fersht 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, Member of Academia Europaea, an Honorary Foreign Member of the American Academy of Arts and Sciences and a Fellow of the Academy of Medical Sciences.

Alan Fersht 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.

Alan Fersht elucidated the leaving-group specificity, leading to a detailed structural interpretation which showed the energetics of "strain" at the binding site.

Alan Fersht demonstrated that their precise specificity depends on consecutive independent recognition steps, and under appropriate conditions he trapped a transiently discharged aminoacyl tRNA.

Alan 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.

Alan Fersht holds honorary doctorates from Uppsala University, Vrije Universiteit Brussel, Weizmann Institute of Science, Hebrew University of Jerusalem, and Aarhus University.

Alan Fersht is an Honorary Fellow of Darwin College, Cambridge and Jesus College, Cambridge.

Herchel Smith Professor of Organic Chemistry at the MRC Centre for Protein Engineering, Cambridge, Sir Alan Fersht is one of the world's leading protein scientists.

Alan Fersht 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.

Alan Fersht's contributions have been widely recognised nationally and internationally by prizes for both chemistry and molecular biology, and by memberships of foreign academies.

Alan Fersht married Marilyn Persell in 1966 and has one son and one daughter.