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Access to the article is free, however registration and sign-in are required. Many protein structures are known with high accuracy, but much less is known about their dynamics. In his Perspective, Falke highlights the report by Eisenmesser et al., who have used a nuclear magnetic resonance approach to follow protein transition state movements during catalysis in the enzyme cyclophilin A. The method should generate a wealth of new information about motions in working enzymes.

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      Keywords:

      NSDL,NSDL_SetSpec_BEN,oai:nsdl.org:2200/20110722030801577T,enzyme catalysis,nuclear magnetic resonance (NMR),protein dynamics

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      English

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      Creative Commons Attribution Non-Commercial Share Alike

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