Where would biology be today without NMR as a structural tool?
There would be 3,000 fewer structures in the protein data bank. We would have quite a different feeling for the way protein molecules behave. We would not have any hands-on information on details of internal dynamics. We would have much less information on folding pathways of proteins, where much of the ground-breaking work has been done at TSRI by the groups of Peter Wright and Jane Dyson. We would not know about solvation of proteins in solution. Quite generally, we would miss a lot of information that is complementary to the data from structure determination by x-ray diffraction in single crystals. You’ve always sought to expand the horizons of NMR, pushing the development of technology not just for your own research, but for the field in general. What are NMR’s current horizons? Where is it going in the next 10, 20 years? We have recently recorded NMR spectra of structures with a size close to one million Daltons, as documented in a Nature article about three months ago. So we now
