NMR structures of membrane proteins in phospholipid bilayers.
Q Rev Biophys. 2014 Jul 17;:1-35
Authors: Radoicic J, Lu GJ, Opella SJ
Abstract
Membrane proteins have always presented technical challenges for structural studies because of their requirement for a lipid environment. Multiple approaches exist including X-ray crystallography and electron microscopy that can give significant insights into their structure and function. However, nuclear magnetic resonance (NMR) is unique in that it offers the possibility of determining the structures of unmodified membrane proteins in their native environment of phospholipid bilayers under physiological conditions. Furthermore, NMR enables the characterization of the structure and dynamics of backbone and side chain sites of the proteins alone and in complexes with both small molecules and other biopolymers. The learning curve has been steep for the field as most initial studies were performed under non-native environments using modified proteins until ultimately progress in both techniques and instrumentation led to the possibility of examining unmodified membrane proteins in phospholipid bilayers under physiological conditions. This review aims to provide an overview of the development and application of NMR to membrane proteins. It highlights some of the most significant structural milestones that have been reached by NMR spectroscopy of membrane proteins, especially those accomplished with the proteins in phospholipid bilayer environments where they function.
PMID: 25032938 [PubMed - as supplied by publisher]
[NMR paper] Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of rotationally aligned membrane proteins in phospholipid bilayers.
J Magn Reson. 2014 Mar 1;242C:224-232
Authors: Das BB, Zhang H, Opella SJ
Abstract
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of heteronuclear dipolar coupling...
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Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of Rotationally Aligned Membrane Proteins in Phospholipid Bilayers
Dipolar Assisted Assignment Protocol (DAAP) for MAS solid-state NMR of Rotationally Aligned Membrane Proteins in Phospholipid Bilayers
Publication date: Available online 1 March 2014
Source:Journal of Magnetic Resonance</br>
Author(s): Bibhuti B. Das , Hua Zhang , Stanley J. Opella</br>
A method for making resonance assignments in magic angle spinning solid-state NMR spectra of membrane proteins that utilizes the range of hetero-nuclear dipolar coupling frequencies in combination with conventional chemical shift based assignment methods is demonstrated. The...
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[NMR paper] Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
Related Articles Resonance assignments of a membrane protein in phospholipid bilayers by combining multiple strategies of oriented sample solid-state NMR.
J Biomol NMR. 2013 Dec 20;
Authors: Lu GJ, Opella SJ
Abstract
Oriented sample solid-state NMR spectroscopy can be used to determine the three-dimensional structures of membrane proteins in magnetically or mechanically aligned lipid bilayers. The...
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[NMR paper] Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Structure Determination of Membrane Proteins in Their Native Phospholipid Bilayer Environment by Rotationally Aligned Solid-State NMR Spectroscopy.
Acc Chem Res. 2013 Jul 5;
Authors: Opella SJ
Abstract
One of the most important topics in experimental structural biology is determining the structures of membrane proteins. These structures represent one-third of all of the information...
[NMR paper] Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimension
Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Related Articles Backbone dynamics of membrane proteins in lipid bilayers: the effect of two-dimensional array formation as revealed by site-directed solid-state 13C NMR studies on Ala- and Val-labeled bacteriorhodopsin.
Biochim Biophys Acta. 2003 Oct 13;1616(2):127-36
Authors: Saitô H, Yamamoto K, Tuzi S, Yamaguchi S
We have recorded...
NMR structures of membrane proteins in phospholipid bilayers.
Linear Mode
