ISMAR mourns the passing of Chris Dobson, who was a friend and colleague of many of us as well as an influential figure in protein NMR and protein science in general. The following obituary was written by Jeff Hoch:
Christopher Martin Dobson died on September 8, 2019, at the age of 69. The cause was cancer. He is survived by his spouse Dr. Mary Dobson and sons Richard and William.
Chris completed his BA, MA, and DPhil degrees at Oxford. Following a research fellowship at Oxford he moved to Harvard in 1977 to assume a junior faculty position in the Department of Chemistry. In 1980 he returned to Oxford, where he remained on the faculty until 2001 when he was named John Humphrey Plummer Professor of Chemical and Structural Biology at the University of Cambridge. Previous holders of Plummer Professorships include Sir John Lennard-Jones and Ray Freeman. In 2007 Chris was elected Master of St. John’s College.
Chris was a Fellow of the Royal Society, a Foreign Associate of the US National Academy of Sciences, an ISMAR Fellow, and the recipient of numerous other awards and honorary degrees. In 2018 he received a Knighthood for his contributions to science and higher education.
Chris was a pioneer in the application of NMR for investigating the structure and dynamics of proteins, a rather audacious undertaking considering he began in the days before multidimensional NMR or stable isotope labeling. Among his early accomplishments were the “convolution difference” procedure for enhancing resolution, assignment of the aromatic region of the proton spectrum of lysozyme and identification of intermediates in the refolding of BPTI, all using exclusively 1D NMR methods.
On his return to the UK from Harvard, Chris continued his investigations of protein dynamics, folding, and unfolding, exploiting the power of then-emerging multidimensional NMR methods and recombinant DNA technology for stable isotope labeling of proteins. His NMR studies of molten globule states of alpha-lactalbumin and other proteins elucidated the dichotomy between order and disorder in proteins, and cooperative and non-cooperative interactions. Inspired by a protein sample that turned to a fibril-containing gel, Chris began to focus on protein misfolding and related diseases, including Alzheimer’s. Among his many contributions in this area, he discovered the mechanisms by which proteins misfold into fibrils, including how protein oligomers nucleate the formation of fibrils, and the neurotoxic role of protein oligomers. He was a co-founder of the Cambridge Centre for Misfolding Diseases in 2013, and of a biotech company (Wren Therapeutics) devoted to protein misfolding diseases in 2016.
While Chris was an avid proponent of the power and versatility of NMR spectroscopy, he often tapped complementary approaches including molecular simulation, mass spectrometry, and even Drosophila. Chris self-deprecatingly referred to his seminal findings on prevention of amyloid-beta (a protein involved in the formation of fibrils in the brains of Alzheimer’s patients) aggregation in Drosophila as “good news for demented fruit flies”. Known for his personal warmth as well as his sense of humor, Chris also had an appreciation for food and wine, introducing his Harvard group to the joys of Spanish Rioja.
In addition to being a prolific scientist and author (more than 800 publications and an astonishing H-index of 135), Chris was a devoted educator, mentor, and advocate for science as a public good. Chris practiced broad scholarship and reveled in intellectual curiosity. The intellectual dialog between Chris and Mary, an expert in medical history, including medieval plagues, is nicely encapsulated in a remarkable joint Darwin College Lecture (University of Cambridge) they delivered in 2014. The online video (available at https://sms.cam.ac.uk/media/1645162) serves as a tribute to Chris and an inspiration to a new generation of scholars.