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

Annamária F. Ángyán, Zoltán Gáspári

Research output: Contribution to journalReview article

22 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)10548-10567
Number of pages20
JournalMolecules
Volume18
Issue number9
DOIs
Publication statusPublished - Sep 1 2013

    Fingerprint

Keywords

  • Dynamic structural ensembles
  • Ensemble generation
  • Molecular dynamics simulation
  • Protein NMR spectroscopy
  • Protein mobility

ASJC Scopus subject areas

  • Analytical Chemistry
  • Chemistry (miscellaneous)
  • Molecular Medicine
  • Pharmaceutical Science
  • Drug Discovery
  • Physical and Theoretical Chemistry
  • Organic Chemistry

Cite this