Linked Life Data

10558871

Source:http://linkedlifedata.com/resource/pubmed/id/10558871

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-12-20
pubmed:abstractText
Thermal denaturation of bovine pancreatic ribonuclease A and a set of its single variants, carrying replacements of hydrophobic residues in the postulated 106-118 chain folding initiation site, has been studied by differential scanning calorimetry. Ribonuclease A variants undergo a two-state thermal transition denaturation except for those with replacement of valine 108. Most mutations cause a significant destabilization of the protein compared to the wild-type, thus demonstrating the importance of hydrophobic residues at the 106-118 region in maintaining the stability of the molecule. Among them, those of valine 108 promote the greatest (14-27 degrees C) destabilization of the molecule. Therefore, valine 108 plays a crucial role for ribonuclease A stability.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
356-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Valine 108, a chain-folding initiation site-belonging residue, crucial for the ribonuclease A stability.
pubmed:affiliation
Laboratori d'Enginyeria de Proteïnes, Departament de Biologia, Facultat de Ciències, Universitat de Girona, Campus Montilivi, Girona, 17071, Spain.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't