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Nature Structural Biology  8, 912 - 914 (2001)
doi:10.1038/nsb1101-912

Protein dynamic studies move to a new time slot

John Cavanagh1 & Ronald A. Venters2

1  John Cavanagh is in the Department of Molecular & Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27695, USA.

2  Ron Venters is in the Duke University NMR Center, Durham, North Carolina 27710, USA.

Correspondence should be addressed to John Cavanagh john_cavanagh@ncsu.edu or Ronald A. Venters rventers@windsurf.mc.duke.edu
Many proteins frequently undergo structural rearrangement to complete their functions. Ligand entry and binding are often associated with some degree of localized disorder. Indeed, low populations of disordered excited states may help drive such processes. Characterization of these states is vital to understanding the mechanisms of many biological functions.

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Protein dynamics from NMR
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Protein dynamics from NMR
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RESEARCH
Studying excited states of proteins by NMR spectroscopy
Nature Structural Biology Letters (01 Nov 2001)

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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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