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Nuclear magnetic resonance (NMR) applied to membrane–protein complexes

Published online by Cambridge University Press:  08 August 2016

Mohammed Kaplan
Affiliation:
NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands
Cecilia Pinto
Affiliation:
NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands
Klaartje Houben
Affiliation:
NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands
Marc Baldus
Affiliation:
NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, The Netherlands
Corresponding
E-mail address:

Abstract

Increasing evidence suggests that most proteins occur and function in complexes rather than as isolated entities when embedded in cellular membranes. Nuclear magnetic resonance (NMR) provides increasing possibilities to study structure, dynamics and assembly of such systems. In our review, we discuss recent methodological progress to study membrane–protein complexes (MPCs) by NMR, starting with expression, isotope-labeling and reconstitution protocols. We review approaches to deal with spectral complexity and limited spectral spectroscopic sensitivity that are usually encountered in NMR-based studies of MPCs. We highlight NMR applications in various classes of MPCs, including G-protein-coupled receptors, ion channels and retinal proteins and extend our discussion to protein–protein complexes that span entire cellular compartments or orchestrate processes such as protein transport across or within membranes. These examples demonstrate the growing potential of NMR-based studies of MPCs to provide critical insight into the energetics of protein–ligand and protein–protein interactions that underlie essential biological functions in cellular membranes.

Type
Review
Copyright
Copyright © Cambridge University Press 2016 

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