Alan R. Fersht
MRC Laboratory of Molecular Biology
Alan Fersht was a Natural Sciences undergraduate and Chemistry postgraduate at Gonville and Caius from 1962-68. He was invited to join LMB as a group leader in 1968 to work on the mechanism of enzymes whose structures were then being solved in the lab and joined a year later after a post-doc at Brandeis with Bill Jencks. He shared room 309 with Max Perutz, who became his mentor. He designed apparatus, which was made in the workshops, to pursue rapid reaction kinetics on enzymes. Alan wrote his book on Enzyme Structure and Mechanism at the end of a bench there with Max’s encouragement between experiments. In 1977, he was appointed Dorothy Hodgkin’s successor as the Wolfson Research Professor of the Royal Society, to be held at Imperial College, where David Blow and Brian Hartley had gone from the LMB. He took up the position after a year’s sabbatical in Arthur Kornberg’s Lab at Stanford to learn gene cloning and DNA replication and proceeded to alienate the organic chemists by the heresy of working on recombinant proteins. In 1981, he began his long collaboration with Greg Winter in developing Protein Engineering, and further alienated the classical enzymologists by working on engineered mutants. In 1988, he was invited back to Cambridge as the Herchel Smith Professor of Organic Chemistry. The MRC, who had supported his work at Imperial College, set him up with the MRC Unit of Protein Function and Design, and almost immediately created the MRC Centre for Protein Engineering (CPE) with Alan as Director and Greg as Deputy Director. The Centre closed and all its staff incorporated into the LMB on his retirement in 2010. Ironically, two of Alan’s students from CPE, Jane Clarke and Sophie Jackson, also became Professors in the Chemistry Department. Both Alan and Greg were knighted for their work on protein engineering and became Masters of Caius and Trinity, respectively, in October 2012, and Jane President of Wolfson in 2018. Alan rejoined the LMB in 2010, where he continued his work on protein folding, misfolding and disease, concentrating on the tumour suppressor p53 until the end of 2017. He was elected FRS in 1983, Honorary Foreign Member of American Academy of Arts and Sciences 5 years later and after another 5 years Foreign Associate National Academy of Sciences (USA), and has been Associate Editor of PNAS since 2000. Among his many prizes have been the Gabor Medal of the Royal Society for Molecular Biology, its Davy Medal for Chemistry and its Royal Medal for his work on protein folding.