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Updated: May 9, 2026

High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
Published on: June 29, 2021
The impact of high hydrostatic pressure on structure and dynamics of β-lactoglobulin
Daniela Russo1, Maria Grazia Ortore, Francesco Spinozzi
1CNR-IOM, c/o Institut Laue-Langevin, Grenoble, France. russo@ill.fr
Methods:
Combining small-angle X-ray and neutron scattering measurements with inelastic neutron scattering experiments, we investigated the impact of high hydrostatic pressure on the structure and dynamics of β-lactoglobulin (βLG) in aqueous solution.
Background:
βLG is a relatively small protein, which is predominantly dimeric in physiological conditions, but dissociates to monomer below about pH3.
Results:
High-pressure structural results show that the dimer-monomer equilibrium, as well as the protein-protein interactions, are only slightly perturbed by pressure, and βLG unfolding is observed above a threshold value of 3000bar. In the same range of pressure, dynamical results put in evidence a slowing down of the protein dynamics in the picosecond timescale and a loss of rigidity of the βLG structure. This dynamical behavior can be related to the onset of unfolding processes, probably promoted from water penetration in the hydrophobic cavity.
General Significance:
Results suggest that density and compressibility of water molecules in contact with the protein are key parameters to regulate the protein flexibility.
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