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Application of Solution NMR Spectroscopy to Study Protein Dynamics

Institute of Chemistry, Organic and Bioorganic Chemistry, University of Graz, Heinrichstrasse 28, A-8010 Graz, Austria
Laboratory of Molecular Biophysics, National Heart, Lung and Blood Institute, National Institutes of Health, 50 South Drive, Bethesda, MD 20892, USA
Author to whom correspondence should be addressed.
Entropy 2012, 14(3), 581-598;
Received: 30 January 2012 / Revised: 13 March 2012 / Accepted: 16 March 2012 / Published: 22 March 2012
(This article belongs to the Special Issue Loop Entropy)
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Recent advances in spectroscopic methods allow the identification of minute fluctuations in a protein structure. These dynamic properties have been identified as keys to some biological processes. The consequences of this structural flexibility can be far‑reaching and they add a new dimension to the structure-function relationship of biomolecules. Nuclear Magnetic Resonance (NMR) spectroscopy allows the study of structure as well as dynamics of biomolecules in a very broad range of timescales at atomic level. A number of new NMR methods have been developed recently to allow the measurements of time scales and spatial fluctuations, which in turn provide the thermodynamics associated with the biological processes. Since NMR parameters reflect ensemble measurements, structural ensemble approaches in analyzing NMR data have also been developed. These new methods in some instances can even highlight previously hidden conformational features of the biomolecules. In this review we describe several solution NMR methods to study protein dynamics and discuss their impact on important biological processes. View Full-Text
Keywords: protein; protein structure; protein dynamics; protein interaction; solution NMR spectroscopy protein; protein structure; protein dynamics; protein interaction; solution NMR spectroscopy

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Göbl, C.; Tjandra, N. Application of Solution NMR Spectroscopy to Study Protein Dynamics. Entropy 2012, 14, 581-598.

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