Partial alignment and measurement of residual dipolar couplings of proteins under high hydrostatic pressure

Fu, Y. and Wand, A. J. (2013) Partial alignment and measurement of residual dipolar couplings of proteins under high hydrostatic pressure. Journal of Biomolecular NMR, 56(4), pp. 353-357. (doi: 10.1007/s10858-013-9754-6)

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Publisher's URL: http://dx.doi.org/10.1007/s10858-013-9754-6

Abstract

High-pressure NMR spectroscopy has emerged as a complementary approach for investigating various structural and thermodynamic properties of macromolecules. Noticeably absent from the array of experimental restraints that have been employed to characterize protein structures at high hydrostatic pressure is the residual dipolar coupling, which requires the partial alignment of the macromolecule of interest. Here we examine five alignment media that are commonly used at ambient pressure for this purpose. We find that the spontaneous alignment of Pf1 phage, d(GpG) and a C12E5/n-hexnanol mixture in a magnetic field is preserved under high hydrostatic pressure. However, DMPC/ DHPC bicelles and collagen gel are found to be unsuitable. Evidence is presented to demonstrate that pressure-induced structural changes can be identified using the residual dipolar coupling.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Fu, Dr Yinan
Authors: Fu, Y., and Wand, A. J.
College/School:College of Medical Veterinary and Life Sciences > School of Molecular Biosciences
Journal Name:Journal of Biomolecular NMR
Publisher:Springer Science+Business Media Dordrecht
ISSN:0925-2738
ISSN (Online):1573-5001
Copyright Holders:Copyright © 2013 Springer Science+Business Media Dordrecht
First Published:First published in Journal of Biomolecular NMR 56(4):353-357
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher.
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