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J Am Chem Soc. 2017 Jan 25;139(3):1065-1068. doi: 10.1021/jacs.6b12089. Epub 2017 Jan 11.

Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.

Author information

1
Institut de Biologie Structurale, Université Grenoble Alpes , 71 Avenue des Martyrs, 38044 Grenoble Cedex 9, France.
2
Commissariat à l'Energie Atomique et aux Energies Alternatives (CEA), Grenoble, France.
3
Centre National de Recherche Scientifique (CNRS), Grenoble, France.
4
Instituto de Investigaciones Químicas (CSIC/US), Sevilla, Spain.

Abstract

NMR spectroscopy is a powerful tool for studying molecular dynamics at atomic resolution simultaneously for a large number of nuclear sites. In this communication, we combine two powerful NMR techniques, relaxation-dispersion NMR and real-time NMR, in order to obtain unprecedented information on the conformational exchange dynamics present in short-lived excited protein states, such as those transiently accumulated during protein folding. We demonstrate the feasibility of the approach for the amyloidogenic protein β2-microglobulin that folds via an intermediate state which is believed to be responsible for the onset of the aggregation process leading to amyloid formation.

PMID:
28067496
DOI:
10.1021/jacs.6b12089
[Indexed for MEDLINE]

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