Andreas, L.B. et al. Proc. Natl. Acad. Sci. USA 113, 9187–9192 (2016).

Magic angle spinning (MAS) solid-state nuclear magnetic resonance (ssNMR) spectroscopy is a useful technique for structure determination, especially of membrane proteins. This method typically requires that protons in proteins be largely replaced with deuterium to reduce spectral overlap. As a result, the method has low sensitivity, and most side chain structures cannot be resolved. Andreas et al. discovered that spinning a sample at a substantially higher speed—that is, 100 kHz or more, as opposed to the more usual ∼50 kHz—greatly reduces the problem of spectral overlap of fully protonated proteins. This allowed them to resolve the structures (including side chains) of two proteins—the model protein GB1 and a viral coat protein—in a relatively short amount of experimental time and using a very small sample.