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

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.

journal_name

J Biomol NMR

journal_title

Journal of biomolecular NMR

authors

Fu Y,Wand AJ

doi

10.1007/s10858-013-9754-6

subject

Has Abstract

pub_date

2013-08-01 00:00:00

pages

353-7

issue

4

eissn

0925-2738

issn

1573-5001

journal_volume

56

pub_type

杂志文章

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