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Title: Mixing and Matching Detergents for Membrane Protein NMR Structure Determination

Abstract

One major obstacle to membrane protein structure determination is the selection of a detergent micelle that mimics the native lipid bilayer. Currently, detergents are selected by exhaustive screening because the effects of protein-detergent interactions on protein structure are poorly understood. In this study, the structure and dynamics of an integral membrane protein in different detergents is investigated by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy and small-angle X-ray scattering (SAXS). The results suggest that matching of the micelle dimensions to the protein's hydrophobic surface avoids exchange processes that reduce the completeness of the NMR observations. Based on these dimensions, several mixed micelles were designed that improved the completeness of NMR observations. These findings provide a basis for the rational design of mixed micelles that may advance membrane protein structure determination by NMR.

Authors:
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  1. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1005636
Resource Type:
Journal Article
Resource Relation:
Journal Name: J. Am. Chem. Soc.; Journal Volume: 131; Journal Issue: (21) ; 06, 2009
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; DETERGENTS; DIMENSIONS; DYNAMICS; ELECTRON SPIN RESONANCE; INTEGRALS; INTERACTIONS; LIPIDS; MEMBRANE PROTEINS; MIXING; NUCLEAR MAGNETIC RESONANCE; PROTEIN STRUCTURE; SMALL ANGLE SCATTERING; SCREENING; SPECTROSCOPY; SURFACES

Citation Formats

Columbus, Linda, Lipfert, Jan, Jambunathan, Kalyani, Fox, Daniel A., Sim, Adelene Y.L., Doniach, Sebastian, Lesley, Scott A., Stanford), Scripps), and UV). Mixing and Matching Detergents for Membrane Protein NMR Structure Determination. United States: N. p., 2009. Web. doi:10.1021/ja808776j.
Columbus, Linda, Lipfert, Jan, Jambunathan, Kalyani, Fox, Daniel A., Sim, Adelene Y.L., Doniach, Sebastian, Lesley, Scott A., Stanford), Scripps), & UV). Mixing and Matching Detergents for Membrane Protein NMR Structure Determination. United States. doi:10.1021/ja808776j.
Columbus, Linda, Lipfert, Jan, Jambunathan, Kalyani, Fox, Daniel A., Sim, Adelene Y.L., Doniach, Sebastian, Lesley, Scott A., Stanford), Scripps), and UV). 2009. "Mixing and Matching Detergents for Membrane Protein NMR Structure Determination". United States. doi:10.1021/ja808776j.
@article{osti_1005636,
title = {Mixing and Matching Detergents for Membrane Protein NMR Structure Determination},
author = {Columbus, Linda and Lipfert, Jan and Jambunathan, Kalyani and Fox, Daniel A. and Sim, Adelene Y.L. and Doniach, Sebastian and Lesley, Scott A. and Stanford) and Scripps) and UV)},
abstractNote = {One major obstacle to membrane protein structure determination is the selection of a detergent micelle that mimics the native lipid bilayer. Currently, detergents are selected by exhaustive screening because the effects of protein-detergent interactions on protein structure are poorly understood. In this study, the structure and dynamics of an integral membrane protein in different detergents is investigated by nuclear magnetic resonance (NMR) and electron paramagnetic resonance (EPR) spectroscopy and small-angle X-ray scattering (SAXS). The results suggest that matching of the micelle dimensions to the protein's hydrophobic surface avoids exchange processes that reduce the completeness of the NMR observations. Based on these dimensions, several mixed micelles were designed that improved the completeness of NMR observations. These findings provide a basis for the rational design of mixed micelles that may advance membrane protein structure determination by NMR.},
doi = {10.1021/ja808776j},
journal = {J. Am. Chem. Soc.},
number = (21) ; 06, 2009,
volume = 131,
place = {United States},
year = 2009,
month =
}
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