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Updated: Jun 7, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
A neutron diffraction study of purple membranes under pressure
Isabelle Gundel Rossand1, Giuseppe Zaccai, Giovanna Fragneto
1Institut de Biologie Structurale, Grenoble, France.
Abstract:
Neutron diffraction from hydrated stacks of natural two-dimensional crystal patches of purple membrane from Halobacterium salinarum was studied as a function of pressure. Measurements in H(2)O and D(2)O permitted the determination of the distribution of water of hydration in the in-plane projection of the membrane. The main experimental difference observed between the samples at 300 MPa and atmospheric pressure was a major reorganization of the hydration around the lipid head groups and protein, associated with a protein conformational change and small reductions in lamellar (stacking) and in-plane lattice spacings, which was consistent with the compressibility of membrane-protein and lipid components.
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