Linked Life Data

21175126

Source:http://linkedlifedata.com/resource/pubmed/id/21175126

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-2-3
pubmed:abstractText
The static light scattering of three globular proteins, bovine serum albumin, ovalbumin, and ovomucoid, and binary mixtures of each protein and trimethylamine oxide (TMAO) containing between 10 and 70% protein, were measured as a function of total weight per volume concentration up to 100 g/L. The observed dependence of scattering upon concentration may be accounted for quantitatively by an effective hard sphere model incorporating an extension that takes into account the nonadditive nature of the repulsive intermolecular interaction between protein and TMAO.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1520-5207
pubmed:author
pubmed:issnType
Electronic
pubmed:day
10
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1289-93
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Effect of nonadditive repulsive intermolecular interactions on the light scattering of concentrated protein-osmolyte mixtures.
pubmed:affiliation
Section on Physical Biochemistry, Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, US Department of Health and Human Services, Bethesda, Maryland 20892, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Intramural