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NMR Spectroscopy in the Analysis of Protein-Protein Interactions

Citation

Gell, DA and Kwan, AN and MAckay, JP, NMR Spectroscopy in the Analysis of Protein-Protein Interactions, Modern Magnetic Resonance, Springer International Publishing, GA Webb (ed), pp. 1-34. ISBN 978-3-319-28275-6 (2017) [Research Book Chapter]


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Abstract

Protein-protein interactions are a central aspect of biology and NMR spectroscopy is one of the most powerful and versatile methods available to characterize their structure, dynamics, kinetics and thermodynamics. In this article, we give an overview of the suite of approaches available to the researcher who wishes to understand their favourite protein-protein interaction in more detail. We begin with an outline of two fundamental concepts that are important for understanding the strengths and limitations of NMR spectroscopy nuclear spin relaxation and chemical exchange. We then present a range of methods including chemical shift perturbation analysis, nuclear Overhauser effects (and its derivatives), residual dipolar couplings, paramagnetic approaches, solid-state NMR and the analysis of low-abundance species. Each method is accompanied by recen texamples from the literature. Together, these techniques can allow both broad and deep insight into the mechanistic underpinnings of protein-protein interactions.

Item Details

Item Type:Research Book Chapter
Keywords:Chemical exchange, Chemical shift perturbation, Cross-saturation, Dark states, Macromolecular NMR spectroscopy, Methyl-TROSY, Protein complexes, Protein-protein interactions
Research Division:Biological Sciences
Research Group:Biochemistry and Cell Biology
Research Field:Structural Biology (incl. Macromolecular Modelling)
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Biological Sciences
Author:Gell, DA (Dr David Gell)
ID Code:122229
Year Published:2017
Deposited By:Medicine (Discipline)
Deposited On:2017-11-06
Last Modified:2017-12-04
Downloads:0

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