NMR spectroscopy brings invisible protein states into focus.

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.

journal_name

Nat Chem Biol

journal_title

Nature chemical biology

authors

Baldwin AJ,Kay LE

doi

10.1038/nchembio.238

subject

Has Abstract

pub_date

2009-11-01 00:00:00

pages

808-14

issue

11

eissn

1552-4450

issn

1552-4469

pii

nchembio.238

journal_volume

5

pub_type

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