obituary (1949–2019) Chris Dobson passed away on September 8th, leaving a wide-reaching legacy. He is best known for revealing the generality of the phenomenon of protein misfolding and aggregation and has provided inspiration for generations of researchers.

hris loved to tell stories, particularly and building a network of connections with those with a lesson in them. One of his the different sectors of our society. In so Cfavorite ones concerned a conversation doing, he took the role of ambassador for the that he had as a young student in Oxford with field of protein misfolding and aggregation, David Phillips, who at the time had recently devoting a significant fraction of his time solved the atomic structure of the first enzyme to traveling and giving lectures, which was using X-ray crystallography. Seeing Chris an activity that he particularly enjoyed. His absorbed in his work in the lab, David asked talks were inspiring both for other scientists him whether he was working on an important and for members of the general public, as he problem. Chris responded that he was trying was able to articulate wonderfully both the to understand the problem, basic science and its impact and to establish prompting David to nod and concede that a close connection with his audience. that was indeed important enough. Perhaps the greatest achievement of Chris, Chris did indeed devote the first part of his however, has been in promoting other people, career to elucidating the problem of protein as he was a uniquely inspiring and dedicated folding, making important contributions that mentor. Time and again, we heard from earned him widespread scientific recognition, people how transformational their encounters including the election to a Fellowship of with Chris were. Despite being very busy, he the Royal Society. What distinguished him always devoted his undivided attention to even more, however, was his work on a the person in front of him and spent what second problem, which was initiated by the Credit: Fran Monks seemed as all the time in the world with observation that, in fact, proteins often do them. Most remarkably, he did so completely not fold correctly, but instead misfold and independently of the seniority of the people aggregate. Initially, this phenomenon was Cambridge with him. There is a special concerned, from the janitors and gardeners of largely considered a nuisance in the lab that atmosphere at the Centre, where for nearly St John’s College, at which he had been Master would typically spoil an experiment. With two decades we have shared ideas, students, for 12 years, to Nobel prize winners and his characteristic perspicacity, however, space and resources in a truly collaborative members of the royal family, whom he also Chris started investigating this behavior manner. More recently, the Centre hosted for visits at St John’s College. His ability more deeply, realizing that “most proteins, moved into the new of Health to help people understand their own talents if not all,” as he liked to say, can end up as building in Cambridge, which Chris was and strengths, as well as the route to fulfilling insoluble aggregates. Textbooks had to be instrumental in establishing and securing them, resulted in some 100 of his former rewritten, he thought, as proteins are only funding for, and which was designed to students and postdocs taking up independent metastable in their native states, while in bring together academic and translational positions at academic institutions in all parts the cellular environment they are effectively research through hosting an incubator of the world. He always thought that his supersaturated, and so possess an inherent space to promote industrial collaborations, success was inextricably linked to that of the tendency to aggregate. as well as shared laboratories to promote people that worked with him. He devoted the last 25 years of his scientific academic collaborations. This initiative Chris has been an inspiring figure for life to uncovering the generality of this resulted in the launch of Wren Therapeutics, generations of scientists. With his unique phenomenon. By establishing novel methods a drug discovery company based on the kindness and attention, and his ability to to study it and by applying these tools and technological innovations following Chris’s provide stability and confidence, he has understanding, his goal was to discover original vision about the fundamental touched and transformed the lives of so therapies for the wide range of human of protein misfolding and aggregation. It is many of those who had the opportunity disorders associated with protein misfolding sobering to think that Chris will not have to meet him through mentoring, advice, and aggregation, which include Alzheimer’s the opportunity to follow this story until its inspiration and above all else his enduring and Parkinson’s disease and type 2 diabetes. full promise will be realized, but his vision passion for science and its ability to solve This work was underpinned by the vision that will live on through these activities. major societal problems. ❐ the key to controlling protein aggregation was The direction that Chris’s scientific to focus on the chemistry and of this activities took clearly illustrates how he Tuomas P. J. Knowles and process rather than its biology. His insight was understood the role of researchers in our that aggregation represents a deviation from society. He recognized that it is a great Centre for Misfolding Diseases, Department of biological function, which happens when privilege to have the opportunity to follow Chemistry, , Cambridge, UK. proteins revert to their fundamental nature as one’s own creativity and that it is important e-mail: [email protected]; [email protected] rather insoluble polypeptide chains. to direct these efforts toward goals that We had the great privilege of establishing could benefit the welfare of people. He thus Published online: 23 January 2020 the Centre for Misfolding Diseases in divided his time between doing research https://doi.org/10.1038/s41589-019-0456-6 Nature | VOL 16 | February 2020 | 105 | www.nature.com/naturechemicalbiology 105