Linked Life Data

10431826

Source:http://linkedlifedata.com/resource/pubmed/id/10431826

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1999-8-26
pubmed:abstractText
Cold shock proteins (Csps) from mesophiles and thermophiles differ widely in their stabilities, but show close structural similarity. Sequence variations involve mainly charged groups, supporting the view that ion pairs contribute significantly to the free energy of stabilization. Based on the known 3D structure of mesophilic Bacillus subtilis CspB and the modeled structure of hyperthermophilic Csp from Thermotoga maritima (TmCsp), D9 and H61 of TmCsp have been substituted by asparagine to find out whether the elimination of predicted ion pairs has a destabilizing effect. Thermal unfolding experiments show that the D9N mutant is destabilized by 9 degrees C, whereas H61N exhibits unaltered wild type behavior. The results are in agreement with preliminary NMR data which confirm the predicted structure only for the N-terminal ion pair.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
454
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-302
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Does the elimination of ion pairs affect the thermal stability of cold shock protein from the hyperthermophilic bacterium Thermotoga maritima?
pubmed:affiliation
Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't