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NMR of Proteins and Small Biomolecules pp 123–185Cite as

Contemporary Methods in Structure Determination of Membrane Proteins by Solution NMR

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Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 326))

Abstract

Integral membrane proteins are vital to life, being responsible for information and material exchange between a cell and its environment. Although high-resolution structural information is needed to understand how these functions are achieved, membrane proteins remain an under-represented subset of the protein structure databank. Solution NMR is increasingly demonstrating its ability to help address this knowledge shortfall, with the development of a diverse array of techniques to counter the challenges presented by membrane proteins. Here we document the advances that are helping to define solution NMR as an effective tool for membrane protein structure determination. Developments introduced over the last decade in the production of isotope-labeled samples, reconstitution of these samples into the growing selection of NMR-compatible membrane-mimetic systems, and the approaches used for the acquisition and application of structural restraints from these complexes are reviewed.

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Abbreviations

β-OG:

β-Octyl glucoside

14-O-PC:

1,2-Di-O-tetradecyl-sn-glycero-3-phosphocholine

6-O-PC:

1,2-Di-O-hexyl-sn-glycero-3-phosphocholine

C6-DHPC:

1,2-Dihexanoyl-sn-glycero-3-phosphocholine

C7-DHPC:

1,2-Diheptanoyl-sn-glycero-3-phosphocholine

CF:

Cell-free

CHAPS:

3-[(3-Cholamidopropyl) dimethylammonio]-1-propanesulfonate

COSY:

Correlation spectroscopy

CSA:

Chemical shift anisotropy

CTAB:

Cetyl-trimethylammonium bromide

DAGK:

Diacylglycerol kinase

DDM:

Dodecylmaltoside

DHAP:

Dihexadecyldimethylammonium bromide

DPC:

Dodecylphosphocholine

DTAB:

Dodecyl-trimethylammonium bromide

EPR:

Electron paramagnetic resonance

gA:

Gramicidin A

GpA:

Glycophorin A

GPCR:

G-protein coupled receptor

HSQC:

Heteronuclear single quantum coherence

LDAO:

Lauryldimethylamine-oxide

LMPC:

Lyso-myristoyl phosphatidylcholine

LMPG:

Lyso-myristoyl phosphatidylglycerol

LPPG:

Lyso-palmitoyl phosphatidylglycerol

MDD:

Multidimensional decomposition

MSP:

Membrane scaffold protein

MTSL:

1-Oxyl-2,2,5,5-tetramethyl-3-pyrroline-3-methyl-methanethiosulfonate

NMR:

Nuclear magnetic resonance

NOE:

Nuclear Overhauser enhancement

NOESY:

Nuclear Overhauser spectroscopy

NUS:

Non-uniform sampling

Omp:

Outer membrane protein

PRE:

Paramagnetic relaxation enhancement

pSRII:

Photosensitive rhodopsin II

RCSA:

Residual chemical shift anisotropy

RDC:

Residual dipolar coupling

SDS:

Sodium dodecyl sulfate

TM:

Transmembrane

TROSY:

Transverse relaxation spectroscopy

UNC2:

Uncoupling protein 2

VDAC:

Voltage dependent anion channel

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Acknowledgments

This work was supported by the Natural Sciences and Engineering Research Council (NSERC).

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  1. Department of Chemistry and Department of Biochemistry, Microbiology and Immunology, University of Ottawa, Ottawa, ON, K1N 6N5, Canada

    Tabussom Qureshi & Natalie K. Goto

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  1. Tabussom Qureshi
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  2. Natalie K. Goto
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Correspondence to Natalie K. Goto .

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  1. , Dept. of Biochemistry, Hong Kong University of Science and Tech, Clear Water Bay, Hong Kong, Kowloon, China, People's Republic

    Guang Zhu

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Qureshi, T., Goto, N.K. (2011). Contemporary Methods in Structure Determination of Membrane Proteins by Solution NMR. In: Zhu, G. (eds) NMR of Proteins and Small Biomolecules. Topics in Current Chemistry, vol 326. Springer, Berlin, Heidelberg. https://doi.org/10.1007/128_2011_306

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