Linked Life Data

10373377

Source:http://linkedlifedata.com/resource/pubmed/id/10373377

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1999-7-28
pubmed:abstractText
Electrostatic contributions to the folding free energy of several hyperthermophilic proteins and their mesophilic homologs are calculated. In all the cases studied, electrostatic interactions are more favorable in the hyperthermophilic proteins. The electrostatic free energy is found not to be correlated with the number of ionizable amino acid residues, ion pairs or ion pair networks in a protein, but rather depends on the location of these groups within the protein structure. Moreover, due to the large free energy cost associated with burying charged groups, buried ion pairs are found to be destabilizing unless they undergo favorable interactions with additional polar groups, including other ion pairs. The latter case involves the formation of stabilizing ion pair networks as is observed in a number of proteins. Ion pairs located on the protein surface also provide stabilizing interactions in a number of cases. Taken together, our results suggest that many hyperthermophilic proteins enhance electrostatic interactions through the optimum placement of charged amino acid residues within the protein structure, although different design strategies are used in different cases. Other physical mechanisms are also likely to contribute, however optimizing electrostatic interactions offers a simple means of enhancing stability without disrupting the core residues characteristic of different protein families.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0022-2836
pubmed:author
pubmed:copyrightInfo
Copyright 1999 Academic Press.
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
289
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1435-44
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Electrostatic contributions to the stability of hyperthermophilic proteins.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY, 10032, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.