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Biochim Biophys Acta. 2013 Oct;1830(10):4974-80. doi: 10.1016/j.bbagen.2013.06.040. Epub 2013 Jul 10.

The impact of high hydrostatic pressure on structure and dynamics of β-lactoglobulin.

Author information

1
CNR-IOM, c/o Institut Laue-Langevin, Grenoble, France. russo@ill.fr

Abstract

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.

KEYWORDS:

Hydrostatic pressure; Neutron scattering; Protein dynamics; Protein folding; Small angle X-ray and neutron scattering

PMID:
23850562
DOI:
10.1016/j.bbagen.2013.06.040
[Indexed for MEDLINE]

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