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