I’m glad to see a letter in today’s Nature commenting on the ‘overly pessimistic’ news feature on 3 February about the first gigahertz nuclear magnetic resonance spectrometer. What should have been a cause for celebration was ruined by a misunderstanding, perhaps even a misrepresentation, of the power and versatility of NMR.
Far from ‘attracting new life to NMR spectroscopy’ — suggesting that the field was on its knees — this investment shows how vibrant this area of research is, at a point when it is poised to make a major contribution to systems biology.
The article describes the world’s most powerful NMR machine, which is now up and running at the European Centre for High Field NMR (CRMN) in Lyon, France. At 1GHz, its magnet is 50 MHz stronger than its nearest rival, and it’s true to say that this a small increase relative to the history of NMR spectrometers, but this misses the point. The question that should have been asked is how powerful are the other machines within that region of France, even within Europe, and what breakthroughs can we expect at this strength?
The Nature news feature mentions that CRMN already has a 900 MHz instrument. But that doesn’t diminish the needed for a stronger magnet. We have barely scratched the surface with regards to structures of membrane proteins, whether they are obtained by crystallography or NMR, and yet these membrane proteins are extremely important for drug research and potential therapy. It’s highly likely that this new machine will begin to make inroads here. But the machine itself can’t solve structures: there are groups around the globe developing techniques that will help produce the structures of larger proteins –look at the paper Science just published.
The worst aspect of this feature is its narrow focus. Yes, NMR works well for small-ish proteins, but the important point is that it offers us opportunities that other techniques don’t. First, it can often produce structures where crystallography has failed. Second, the structure is obtained in solution, allowing us to see a dynamic picture. Third, it’s the only technique that allows us to detect weak, transient interactions, which will be vital for building up a picture of protein-protein and protein-ligand interactions for systems biology and beyond. And fourth, the first in-cell NMR structures were reported about 6 months ago – this will revolutionise our understanding of structures within the cell.
NMR protein spectroscopy is well and truly alive and kicking. So smile, Lyndon Emsley – for goodness sake! You’ve just installed the world’s most powerful NMR machine, worth $16.3 million. In the news feature, you look like you’ve just lost the winning Euro-millions lottery ticket.