Linked Life Data

9168948

Source:http://linkedlifedata.com/resource/pubmed/id/9168948

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-6-30
pubmed:abstractText
The phage P22 tailspike protein is one of the few proteins for which both in vivo and in vitro folding pathways have been thoroughly characterized. Many temperature-sensitive folding (tsf) mutations that cause the mutant tailspike polypeptides not to be folded at high restrictive temperatures have been identified. One-third of the tsf mutation sites are located in one domain called the dorsal fin domain (residues 197-259), which protrudes on the solvent-exposed side of the main beta helix. In the present study, we introduced various amino acid substitutions at three tsf mutation sites (residue numbers 235, 238, and 244) in this domain to elucidate the mechanism of these tsf mutations in detail. The side-chain specificity at these tsf sites, together with structural examination in the tertiary fold, strongly suggests that destabilization of folding intermediates by loss of specific interactions is likely to be the major cause of the tsf defect in the dorsal fin domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
233
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
857-62
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Side-chain specificity at three temperature-sensitive folding mutation sites of P22 tailspike protein.
pubmed:affiliation
Division of Protein Engineering, Korea Research Institute of Bioscience and Biotechnology, KIST, Yusong, Taejon, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't