Open Access Repository

NMR Spectroscopy in the Analysis of Protein-Protein Interactions

Gell, DA ORCID: 0000-0003-0382-1181, Kwan, AN and MAckay, JP 2018 , 'NMR Spectroscopy in the Analysis of Protein-Protein Interactions', in GA Webb (ed.), Modern Magnetic Resonance , Springer International Publishing, pp. 1-34.

Full text not available from this repository.


Protein-protein interactions are a central aspect of biology and NMR spectroscopyis one of the most powerful and versatile methods available to characterizetheir structure, dynamics, kinetics and thermodynamics. In this article, we give anoverview of the suite of approaches available to the researcher who wishes tounderstand their favourite protein-protein interaction in more detail. We beginwith an outline of two fundamental concepts that are important for understandingthe strengths and limitations of NMR spectroscopy – nuclear spin relaxation andchemical exchange. We then present a range of methods including chemical shiftperturbation analysis, nuclear Overhauser effects (and its derivatives), residualdipolar couplings, paramagnetic approaches, solid-state NMR and the analysis oflow-abundance species. Each method is accompanied by recen texamples fromthe literature. Together, these techniques can allow both broad and deep insightinto the mechanistic underpinnings of protein-protein interactions.

Item Type: Book Section
Authors/Creators:Gell, DA and Kwan, AN and MAckay, JP
Keywords: Chemical exchange, Chemical shift perturbation, Cross-saturation, Dark states, Macromolecular NMR spectroscopy, Methyl-TROSY, Protein complexes, Protein-protein interactions
Publisher: Springer International Publishing
DOI / ID Number: 10.1007/978-3-319-28275-6_121-1
Copyright Information:

Copyright 2017 Springer International Publishing AG

Related URLs:
Item Statistics: View statistics for this item

Actions (login required)

Item Control Page Item Control Page