Literature DB >> 28709996

Applications of solid-state NMR to membrane proteins.

Vladimir Ladizhansky1.   

Abstract

Membrane proteins mediate flow of molecules, signals, and energy between cells and intracellular compartments. Understanding membrane protein function requires a detailed understanding of the structural and dynamic properties involved. Lipid bilayers provide a native-like environment for structure-function investigations of membrane proteins. In this review we give a general discourse on the recent progress in the field of solid-state NMR of membrane proteins. Solid-state NMR is a variation of NMR spectroscopy that is applicable to molecular systems with restricted mobility, such as high molecular weight proteins and protein complexes, supramolecular assemblies, or membrane proteins in a phospholipid environment. We highlight recent advances in applications of solid-state NMR to membrane proteins, specifically focusing on the recent developments in the field of Dynamic Nuclear Polarization, proton detection, and solid-state NMR applications in situ (in cell membranes). This article is part of a Special Issue entitled: Biophysics in Canada, edited by Lewis Kay, John Baenziger, Albert Berghuis and Peter Tieleman.
Copyright © 2017 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Cell membrane; Dynamic Nuclear Polarization; In situ solid-state NMR; Lipid bilayer; Membrane protein; Protein structure; Solid-state NMR

Mesh:

Substances:

Year:  2017        PMID: 28709996     DOI: 10.1016/j.bbapap.2017.07.004

Source DB:  PubMed          Journal:  Biochim Biophys Acta Proteins Proteom        ISSN: 1570-9639            Impact factor:   3.036


  17 in total

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5.  A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.

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