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Biophys J. 2019 May 7;116(9):1682-1691. doi: 10.1016/j.bpj.2019.03.019. Epub 2019 Mar 30.

The Fluidity of Phosphocholine and Maltoside Micelles and the Effect of CHAPS.

Author information

1
Department of Chemistry, University of Virginia, Charlottesville, Virginia.
2
Department of Biological Sciences and Centre for Molecular Simulation, University of Calgary, Calgary, Alberta, Canada.
3
Department of Chemistry, University of Virginia, Charlottesville, Virginia. Electronic address: columbus@virginia.edu.

Abstract

The dynamics of phosphocholine and maltoside micelles, detergents frequently used for membrane protein structure determination, were investigated using electron paramagnetic resonance of spin probes doped into the micelles. Specifically, phosphocholines are frequently used detergents in NMR studies, and maltosides are frequently used in x-ray crystallography structure determination. Beyond the structural and electrostatic differences, this study aimed to determine whether there are differences in the local chain dynamics (i.e., fluidity). The nitroxide probe rotational dynamics in longer chain detergents is more restricted than in shorter chain detergents, and maltoside micelles are more restricted than phosphocholine micelles. Furthermore, the micelle microviscosity can be modulated with mixtures, as demonstrated with mixtures of 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate with n-dodecylphosphocholine, n-tetradecylphosphocholine, n-decyl-β-D-maltoside, or n-dodecyl-β-D-maltoside. These results indicate that observed differences in membrane protein stability in these detergents could be due to fluidity in addition to the already determined structural differences.

PMID:
31023535
PMCID:
PMC6506624
[Available on 2020-05-07]
DOI:
10.1016/j.bpj.2019.03.019

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