Abstract
MethodsCombining 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. BackgroundβLG is a relatively small protein, which is predominantly dimeric in physiological conditions, but dissociates to monomer below about pH3. ResultsHigh-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 significanceResults 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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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - General Subjects
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