http://www.cnr.it/ontology/cnr/individuo/prodotto/ID263023
The impact of high hydrostatic pressure on structure and dynamics of ?-lactoglobulin (Articolo in rivista)
- Type
- Label
- The impact of high hydrostatic pressure on structure and dynamics of ?-lactoglobulin (Articolo in rivista) (literal)
- Anno
- 2013-01-01T00:00:00+01:00 (literal)
- Alternative label
Daniela Russoa,
Maria Grazia Ortore
Francesco Spinozzi
Paolo Marianic,
Camille Loupiac
Burkhard Annighofer
Alessandro Paciaronig, (2013)
The impact of high hydrostatic pressure on structure and dynamics of ?-lactoglobulin
in Biochimica et biophysica acta. G, General subjects (Print)
(literal)
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- Daniela Russoa,
Maria Grazia Ortore
Francesco Spinozzi
Paolo Marianic,
Camille Loupiac
Burkhard Annighofer
Alessandro Paciaronig, (literal)
- Pagina inizio
- Pagina fine
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- Rivista
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- PAPC, UMR PAM, AgroSup Dijon-Université de Bourgogne, Dijon, France
Department of Life and Environmental Sciences, Marche Polytechnic University, Ancona, Italy
Department of Physics, University of Perugia, Perugia, Italy
Laboratoire Léon Brillouin, Saclay CEA, Paris, France
CNR-IOM, c/o Institut Laue-Langevin, Grenoble, France
Institut Lumière Matière, Université de Lyon 1, France (literal)
- Titolo
- The impact of high hydrostatic pressure on structure and dynamics of ?-lactoglobulin (literal)
- 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 ?-lactoglobulin (?LG) in aqueous solution.
Background
?LG is a relatively small protein, which is predominantly dimeric in physiological conditions, but dissociates to monomer below about pH 3.
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 ?LG unfolding is observed above a threshold value of 3000 bar. 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 ?LG 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;
Protein folding;
Protein dynamics;
Neutron scattering;
Small angle X-ray and neutron scattering (literal)
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