Linked Life Data

9127936

Source:http://linkedlifedata.com/resource/pubmed/id/9127936

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
1997-5-27
pubmed:abstractText
The stabilization of ribonuclease A by alpha-alpha-trehalose was studied by preferential interaction and thermal unfolding. The protein is stabilized by trehalose at pH 2.8 and pH 5.5. Wyman linkage analysis showed increased exclusion of trehalose from the protein domain on denaturation. Preferential interaction measurements were carried out at 52 degrees C at pH 5.5 and 2.8, where the protein is native and unfolded, respectively, and at 20 degrees C where the protein is native at both pH values. At the low temperature, the interaction was preferential exclusion. At 52 degrees C the interaction was that of preferential binding, greater to the native than the unfolded protein, the increment on denaturation being identical to that deduced from the Wyman analysis. The stabilizing effect of trehalose can be fully accounted by the change in transfer free energy on unfolding. The temperature dependence of the preferential interactions of 0.5 M trehalose with ribonuclease A showed that it is the smaller preferential binding to the unfolded protein than to the native one which gives rise to the stabilization. A thermodynamic analysis of the data led to approximate values of the transfer enthalpies and transfer entropies for the trehalose-ribonuclease A system.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0301-4622
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
64
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25-43
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The thermodynamic mechanism of protein stabilization by trehalose.
pubmed:affiliation
Graduate Department of Biochemistry, Brandeis University, Waltham, Massachusetts 02254, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.