Linked Life Data

16337234

Source:http://linkedlifedata.com/resource/pubmed/id/16337234

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2006-2-28
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:volume
1764
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
211-6
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
beta-lactoglobulin under high pressure studied by small-angle neutron scattering.
pubmed:affiliation
Equipe d'Ingénierie Moléculaire et Sensorielle des Aliments et des Produits de Santé, ENSBANA, Dijon, France. camille.loupiac@u-bourgogne.fr
pubmed:publicationType
Journal Article