Ensemble-based interpretations of NMR structural data to describe protein internal dynamics

Kovácsné Ángyán Annamária Franciska

Gáspári Zoltán

2013

01.04. Kémiai tudományok

NMR spectroscopy is the leading technique to characterize protein internal dynamics at the atomic level and on multiple time scales. However, the structural interpretation of the observables obtained by various measurements is not always straightforward and in many cases dynamics-related parameters are only used to “decorate” static structural models without offering explicit description of conformational heterogeneity. To overcome such limitations, several computational techniques have been developed to generate ensemble-based representations of protein structure and dynamics with the use of NMR-derived data. An important common aspect of the methods is that NMR observables and derived parameters are interpreted as properties of the ensemble instead of individual conformers. The resulting ensembles reflect the experimentally determined internal mobility of proteins at a given time scale and can be used to understand the role of internal motions in biological processes at atomic detail. In this review we provide an overview of the calculation methods currently available and examples of biological insights obtained by the ensemble-based models of the proteins investigated.

angol

angol

Folyóiratcikk

PeerReviewed

text

https://publikacio.ppke.hu/id/eprint/1453/1/molecules-18-10548.pdf

Kovácsné Ángyán Annamária Franciska; Gáspári Zoltán: Ensemble-based interpretations of NMR structural data to describe protein internal dynamics. MOLECULES, 18 (9). pp. 10548-10567. ISSN 1420-3049 (2013)

MTMT:2387256 10.3390/molecules180910548

https://publikacio.ppke.hu/id/eprint/1453/

https://doi.org/10.3390/molecules180910548

MTMT:2387256 10.3390/molecules180910548