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231224s2014 xx |||||o 00| ||eng c |
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|a 10.1016/j.pnmrs.2014.07.001
|2 doi
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|a DE-627
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|e rakwb
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|a eng
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|a Wang, Shenlin
|e verfasserin
|4 aut
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|a Recent advances in magic angle spinning solid state NMR of membrane proteins
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|c 2014
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|a Text
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|a ƒaComputermedien
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|a ƒa Online-Ressource
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|a Date Completed 28.09.2015
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|a Date Revised 02.12.2014
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Copyright © 2014 Elsevier B.V. All rights reserved.
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|a Membrane proteins mediate many critical functions in cells. Determining their three-dimensional structures in the native lipid environment has been one of the main objectives in structural biology. There are two major NMR methodologies that allow this objective to be accomplished. Oriented sample NMR, which can be applied to membrane proteins that are uniformly aligned in the magnetic field, has been successful in determining the backbone structures of a handful of membrane proteins. Owing to methodological and technological developments, Magic Angle Spinning (MAS) solid-state NMR (ssNMR) spectroscopy has emerged as another major technique for the complete characterization of the structure and dynamics of membrane proteins. First developed on peptides and small microcrystalline proteins, MAS ssNMR has recently been successfully applied to large membrane proteins. In this review we describe recent progress in MAS ssNMR methodologies, which are now available for studies of membrane protein structure determination, and outline a few examples, which highlight the broad capability of ssNMR spectroscopy
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Review
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|a Lipid bilayer
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|a Magic angle spinning solid-state NMR
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|a Membrane protein
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|a Multidimensional NMR
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|a Protein structure
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|a Lipid Bilayers
|2 NLM
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|a Membrane Proteins
|2 NLM
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|a Ladizhansky, Vladimir
|e verfasserin
|4 aut
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|i Enthalten in
|t Progress in nuclear magnetic resonance spectroscopy
|d 1998
|g 82(2014) vom: 04. Okt., Seite 1-26
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|x 1873-3301
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|g volume:82
|g year:2014
|g day:04
|g month:10
|g pages:1-26
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|u http://dx.doi.org/10.1016/j.pnmrs.2014.07.001
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