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Synergistic use of NMR and MD simulations to study the structural heterogeneity of proteins
Author(s) -
EstebanMartín Santiago,
Bryn Fenwick Robert,
Salvatella Xavier
Publication year - 2012
Publication title -
wiley interdisciplinary reviews: computational molecular science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.126
H-Index - 81
eISSN - 1759-0884
pISSN - 1759-0876
DOI - 10.1002/wcms.1093
Subject(s) - molecular dynamics , monte carlo method , complementarity (molecular biology) , nuclear magnetic resonance spectroscopy , statistical physics , macromolecule , characterization (materials science) , chemistry , biological system , computer science , computational chemistry , physics , nanotechnology , nuclear magnetic resonance , materials science , biology , mathematics , genetics , biochemistry , statistics
Nuclear magnetic resonance spectroscopy (NMR) and molecular dynamics (MD) simulations are powerful techniques for the structural characterization of macromolecules. NMR is unique in its ability to provide experimental information at atomic level on the structure as well as on the amplitude and rate of structural fluctuations. MD provides physically sound models and potential mechanisms that connect conformations in time. Nevertheless, none of these techniques allow yet obtaining experimentally validated movies of protein motions at atomic resolution. Instead, it is their complementarity and synergy which offer a unique opportunity toward this end. Here, we overview recent examples that illustrate how much these two techniques benefit from each other, both passively and actively, for the characterization of the structural heterogeneity in proteins. © 2012 John Wiley & Sons, Ltd. This article is categorized under: Molecular and Statistical Mechanics > Molecular Dynamics and Monte-Carlo Methods