Document Detail

beta-lactoglobulin under high pressure studied by small-angle neutron scattering.
MedLine Citation:
PMID:  16337234     Owner:  NLM     Status:  MEDLINE    
We used small-angle neutron scattering to study the effects of the high hydrostatic pressure on the structure of beta-lactoglobulin. Experiments were carried out at pH 7 on the dimeric form of the protein in a pressure range going from 50 MPa to 300 MPa. These measurements allow the protein size and the interactions between macromolecules to be studied during the application of pressure. Increasing pressure up to 150 MPa leads to a swollen state of the protein that gives rise to an increase of the radius of gyration by about 7%. Within this pressure range, we also show that the interaction between macromolecules weakens although it remains repulsive. The measurements show an aggregation process occurring above 150 MPa. From the spectra analysis, it appears that the aggregation occurs mainly by association of the dimeric units.
C Loupiac; M Bonetti; S Pin; P Calmettes
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Publication Detail:
Type:  Journal Article     Date:  2005-11-07
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  1764     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-28     Completed Date:  2006-04-19     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  Netherlands    
Other Details:
Languages:  eng     Pagination:  211-6     Citation Subset:  IM    
Equipe d'Ingénierie Moléculaire et Sensorielle des Aliments et des Produits de Santé, ENSBANA, Dijon, France.
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MeSH Terms
Hydrogen-Ion Concentration
Hydrostatic Pressure
Lactoglobulins / chemistry*
Neutron Diffraction
Protein Folding
Scattering, Radiation
Reg. No./Substance:

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