Linked Life Data

9828007

Source:http://linkedlifedata.com/resource/pubmed/id/9828007

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1999-1-21
pubmed:abstractText
The stability of the N-terminal domain of the ribosomal protein L9, NTL9, from Bacillus stearothermophilus has been monitored by circular dichroism at various temperatures and chemical denaturant concentrations in H2O and D2O. The basic thermodynamic parameters for the unfolding reaction, deltaH(o), deltaS(o), and deltaC(o)p, were determined by global analysis of temperature and denaturant effects on stability. The data were well fit by a model that assumes stability varies linearly with denaturant concentration and that uses the Gibbs-Helmholtz equation to model changes in stability with temperature. The results obtained from the global analysis are consistent with information obtained from individual thermal and chemical denaturations. NTL9 has a maximum stability of 3.78 +/- 0.25 kcal mol(-1) at 14 degrees C. DeltaH(o)(25 degrees C) for protein unfolding equals 9.9 +/- 0.7 kcal mol(-1) and TdeltaS(o)++(25 degrees C) equals 6.2 +/- 0.6 kcal mol(-1). DeltaC(o)p equals 0.53 +/- 0.06 kcal mol(-1) deg(-1). There is a small increase in stability when D2O is substituted for H2O. Based on the results from global analysis, NTL9 is 1.06 +/- 0.60 kcal mol(-1) more stable in D2O at 25 degrees C and Tm is increased by 5.8 +/- 3.6 degrees C in D2O. Based on the results from individual denaturation experiments, NTL9 is 0.68 +/- 0.68 kcal mol(-1) more stable in D2O at 25 degrees C and Tm is increased by 3.5 +/- 2.1 degrees C in D2O. Within experimental error there are no changes in deltaH(o) (25 degrees C) when D2O is substituted for H2O.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-1652762, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-5531188, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-5845676, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-7552708, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-8306963, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-8561051, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-8639557, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-8784192, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-8980686, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9000630, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9153419, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9214287, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9377710, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9380687, http://linkedlifedata.com/resource/pubmed/commentcorrection/9828007-9454593
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0961-8368
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2405-12
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Global analysis of the thermal and chemical denaturation of the N-terminal domain of the ribosomal protein L9 in H2O and D2O. Determination of the thermodynamic parameters, deltaH(o), deltaS(o), and deltaC(o)p and evaluation of solvent isotope effects.
pubmed:affiliation
Department of Chemistry, State University of New York at Stony Brook, 11794-3400, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't