Linked Life Data

21186800

Source:http://linkedlifedata.com/resource/pubmed/id/21186800

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-2-3
pubmed:abstractText
Preferential interaction coefficients provide a thermodynamic measure to quantify the interactions between cosolutes and a protein. Preferential interactions of cosolutes can be measured experimentally using dialysis/densimetry and vapor pressure osmometry (VPO) techniques. The cosolute arginine is a widely used aggregation suppressor with a seemingly unique behavior. Its role in protein aggregation has been studied extensively, although a complete mechanistic understanding of its behavior is lacking. Moreover, due to experimental limitations, experimental preferential interaction data for arginine has only been reported at low concentrations. Schneider and Trout ( J. Phys. Chem. B 2009 , 113 , 7 ) have reported experimental preferential interaction data for argHCl (up to 0.7 m), and their study raised several interesting questions about the preferential interaction of arginine with proteins. Arginine is attracted to proteins at low concentrations but it was highly excluded at high concentrations. Furthermore, the preferential interaction coefficient values were found to vary as a square of the concentration, which is different from commonly observed linear relationship for other cosolutes like urea, glycerol, guanidinium hydrochloride, etc. In this study, preferential interaction coefficients of argHCl have been estimated computationally for two proteins (lysozyme and ?-chymotripsinogen A) for a large concentration range (up to 2.8 m). On the basis of these results, the molecular level interactions responsible for the nonlinear exclusion of arginine from the protein surface are identified.
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
1243-53
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Preferential interaction coefficients of proteins in aqueous arginine solutions and their molecular origins.
pubmed:affiliation
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't