[3] "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".Dobson authored and co-authored over 800 papers and review articles,[8] including 38 in Nature, Science and Cell, which have been cited over 100,000 times.

[15][16] His nomination reads: 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.

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.

[8] "All text published under the heading 'Biography' on Fellow profile pages is available under Creative Commons Attribution 4.0 International License.” --Royal Society Terms, conditions and policies at the Wayback Machine (archived 11 November 2016)