The impact of high hydrostatic pressure on structure and dynamics of ß-lactoglobulin.
Biochim Biophys Acta
; 1830(10): 4974-80, 2013 Oct.
Article
em En
| MEDLINE
| ID: mdl-23850562
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 ß-lactoglobulin (ßLG) in aqueous solution.BACKGROUND:
ßLG 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 ßLG 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 ßLG structure. This dynamical behavior can be related to the onset of unfolding processes, probably promoted from water penetration in the hydrophobic cavity. GENERALSIGNIFICANCE:
Results suggest that density and compressibility of water molecules in contact with the protein are key parameters to regulate the protein flexibility.Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pressão Hidrostática
/
Lactoglobulinas
Idioma:
En
Revista:
Biochim Biophys Acta
Ano de publicação:
2013
Tipo de documento:
Article
País de afiliação:
França