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Review
. 2009 Nov;5(11):808-14.
doi: 10.1038/nchembio.238.

NMR spectroscopy brings invisible protein states into focus

Andrew J Baldwin  1 , Lewis E Kay
Affiliations
Review

NMR spectroscopy brings invisible protein states into focus

Andrew J Baldwin et al. Nat Chem Biol. 2009 Nov.

Abstract

Molecular dynamics are essential for protein function. In some cases these dynamics involve the interconversion between ground state, highly populated conformers and less populated higher energy structures ('excited states') that play critical roles in biochemical processes. Here we describe recent advances in NMR spectroscopy methods that enable studies of these otherwise invisible excited states at an atomic level and that help elucidate their important relation to function. We discuss a range of examples from molecular recognition, ligand binding, enzyme catalysis and protein folding that illustrate the role that motion plays in 'funneling' conformers along preferred pathways that facilitate their biological function.

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