Sparsely populated transient states of proteins and their complexes play an important role in many biological processes including protein–protein and protein–DNA recognition, allostery, conformational selection, induced fit and self-assembly. These states are difficult to study as their low population and transient nature makes them effectively invisible to conventional structural and biophysical techniques. In the present article, I summarize recent NMR developments in our laboratory, including the use of paramagnetic relaxation enhancement, lifetime line broadening and dark-state exchange saturation transfer spectroscopy, that have permitted such sparsely populated states to be detected, characterized and, in some instances, visualized. I illustrate the application of these methods to the elucidation of mechanisms whereby transcription factors locate their specific target sites within an overwhelming sea of non-specific DNA, to the characterization of encounter complexes in protein–protein recognition, to large-scale interdomain motions involved in ligand binding, and to the interaction of monomeric amyloid β-peptide with the surface of amyloid protofibrils and the internal cavity surface of the chaperonin GroEL.
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Conference Article|
November 20 2013
Seeing the invisible by paramagnetic and diamagnetic NMR
G. Marius Clore
G. Marius Clore
1
*Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, U.S.A.
1emailmariusc@mail.nih.gov
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Publisher: Portland Press Ltd
Received:
September 20 2013
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem Soc Trans (2013) 41 (6): 1343–1354.
Article history
Received:
September 20 2013
Citation
G. Marius Clore; Seeing the invisible by paramagnetic and diamagnetic NMR. Biochem Soc Trans 1 December 2013; 41 (6): 1343–1354. doi: https://doi.org/10.1042/BST20130232
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