Direct observation of hierarchical protein dynamics

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Science  01 May 2015:
Vol. 348, Issue 6234, pp. 578-581
DOI: 10.1126/science.aaa6111

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A hierarchy of protein motions

Functioning proteins are not static but explore complex conformational energy landscapes. Lewandowski et al. used multinuclear solid-state nuclear magnetic resonance experiments to measure protein motion over a broad range of temperatures and time scales. Above 160 K there was a strong coupling between solvent and protein motion. The hierarchy of motions as the temperature increased revealed the dynamic modes that relate solvent, sidechain, and backbone motion.

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