17 Facts About Chris Dobson

Dobson was born on 8 October 1949 in Rinteln, Germany, where his father, Arthur Dobson was commissioned as an officer.

Christopher Dobson was educated at Hereford Cathedral Junior School, and then Abingdon School from 1960 until 1967.

Chris Dobson completed a Master of Arts and Doctor of Philosophy at the University of Oxford, where he was a student of Keble College, Oxford and Merton College, Oxford.

Chris Dobson is well known for his serendipitous discovery that ordinary proteins can misfold and aggregate to form amyloid structures.

Chris Dobson authored and co-authored over 800 papers and review articles, including 38 in Nature, Science and Cell, which have been cited over 100,000 times.

Chris Dobson held research fellowships at Merton College, Oxford and then Linacre College, Oxford before working at Harvard University.

Chris Dobson returned to Oxford in 1980 as a Fellow of Lady Margaret Hall, Oxford and as a University Lecturer in Chemistry, later receiving promotions to Reader, then Professor of Chemistry in 1996.

Chris Dobson moved to the University of Cambridge in 2001 as the John Humphrey Plummer Professor of Chemical and Structural Biology.

In 2012, Chris Dobson founded the Cambridge Centre for Misfolding Diseases, which is currently based in the Chemistry of Health building at the Department of Chemistry at the University of Cambridge.

Chris Dobson was knighted in the 2018 Queen's Birthday Honours for his contributions to science and higher education.

In 2009, Chris Dobson was awarded the Royal Medal by the Royal Society "for his outstanding contributions to the understanding of the mechanisms of protein folding and mis-folding, and the implications for disease", and in 2014 he received both the Heineken Prize for Biochemistry and Biophysics and the Feltrinelli International Prize for Medicine.

Chris Dobson was elected a Fellow of the Royal Society in 1996.

Chris Dobson is distinguished for his studies, principally using NMR methods, of the structures and dynamics of proteins in solution.

Such studies include those on lysozyme, with which he demonstrated many methodological advances, interleukin-4, with which he established for the first time the topology of the important family of haemopoietic helical cytokines, and urokinase-type plasminogen activator, with which he elucidated the dynamic characteristics of multidomain fibrinolytic proteins, Chris Dobson is a pioneer in the application of NMR methods to the problem of protein folding, which is the major theme of his work.

Chris Dobson has explored the properties and reactions of molecules in solids by means of NMR spectroscopy, including proteins, organometallic compounds, inorganic paramagnets and the silicaceous components of hydraulic materials.

Chris Dobson mentored and supervised many notable PhD students and post-doctoral researchers, many of whom became renowned experts in their own field.

Chris Dobson died on 8 September 2019, from cancer, at Royal Marsden Hospital in Sutton, near Surrey.