Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation-Dispersion NMR.
J Am Chem Soc
; 139(3): 1065-1068, 2017 01 25.
Article
em En
| MEDLINE
| ID: mdl-28067496
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 ß2-microglobulin that folds via an intermediate state which is believed to be responsible for the onset of the aggregation process leading to amyloid formation.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Microglobulina beta-2
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Ressonância Magnética Nuclear Biomolecular
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Simulação de Dinâmica Molecular
Limite:
Humans
Idioma:
En
Ano de publicação:
2017
Tipo de documento:
Article