Dobson was born on 8 October 1949 in Germany, where his father, Arthur Dobson was commissioned as an officer. Both Arthur Dobson and Christopher Dobson's mother, Mabel Dobson (née Pollard), were originally from Bradford in Yorkshire and had left school at age 14. Dobson had two older siblings, Graham and Gillian. Due to his father's postings, Dobson also lived in Lagos, Nigeria.
Dobson's research largely focused on protein folding and protein misfolding, and its association with medical disorders particularly Alzheimer's and Parkinson's diseases. By applying chemical and biophysical techniques, Dobson investigated links between protein structure, function, and disease.
He is well-known for his serendipitous discovery that ordinary proteins can misfold and aggregate to form amyloid structures.
“A postdoc who left his sample of an unfolded protein in an NMR [nuclear magnetic resonance] spectrometer over a long weekend discovered, on his return, that it had turned into a gel. We were curious about this phenomenon and found that the NMR tube was full of amyloid fibrils that we then thought were associated only with diseases.”
In 2012, 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.
In 2016, Chris Dobson co-founded Wren Therapeutics, a biotechnology start-up company whose mission is to find new therapeutics for Alzheimer's disease.
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, Dobson is a pioneer in the application of NMR methods to the problem of protein folding, which is now the major theme of his work. His studies on lysozyme are resulting in one of the most detailed descriptions of a folding pathway for a protein. Dobson has explored the properties and reactions of molecules in solids by means of NMR spectroscopy, including proteins, organometallic compounds, inorganicparamagnets and the silicaceous components of hydraulic materials. Notable here are analyses of the nature and origin of dynamic properties in molecular solids, and their relationship to structure and reactivity.