Titel
NMR Methods to Study Dynamic Allostery
Autor*in
Sarina Grutsch
Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck
Martin Tollinger
Institute of Organic Chemistry, Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck
Abstract
Nuclear magnetic resonance (NMR) spectroscopy provides a unique toolbox of experimental probes for studying dynamic processes on a wide range of timescales, ranging from picoseconds to milliseconds and beyond. Along with NMR hardware developments, recent methodological advancements have enabled the characterization of allosteric proteins at unprecedented detail, revealing intriguing aspects of allosteric mechanisms and increasing the proportion of the conformational ensemble that can be observed by experiment. Here, we present an overview of NMR spectroscopic methods for characterizing equilibrium fluctuations in free and bound states of allosteric proteins that have been most influential in the field. By combining NMR experimental approaches with molecular simulations, atomistic-level descriptions of the mechanisms by which allosteric phenomena take place are now within reach.
Stichwort
NMR relaxationNMR spectroscopyMolecular dynamicsDNA-binding proteinsAllosteric regulationAbsorption spectroscopyProtein complexesRelaxation (physics)
Objekt-Typ
Sprache
Englisch [eng]
Persistent identifier
Erschienen in
Titel
PLOS Computational Biology
Band
12
Ausgabe
3
Publication
Public Library of Science (PLoS)
Erscheinungsdatum
2016
Zugänglichkeit
Rechte
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