Literature DB >> 19425578

Mixing and matching detergents for membrane protein NMR structure determination.

Linda Columbus1, Jan Lipfert, Kalyani Jambunathan, Daniel A Fox, Adelene Y L Sim, Sebastian Doniach, Scott A Lesley.   

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.

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Year:  2009        PMID： 19425578      PMCID： PMC2751809          DOI： 10.1021/ja808776j

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


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