Linked Life Data

2696341

Source:http://linkedlifedata.com/resource/pubmed/id/2696341

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-3-27
pubmed:abstractText
The three-dimensional structure of a protein is governed by the thermodynamical principle established experimentally by Anfinsen, Isemura, and others. The rapidity of the folding process is another important key phenomenon. With these basics in mind an island model is proposed which requires a restricted folding pathway. A physicochemical method of the prediction of alpha-helices and beta-strands is also discussed. By virtue of the long-range hydrophobic interaction and the specific interactions between hydrophobic residues which are determined by the basic idea underlying the island model, one can fold the polypeptide chain into a tertiary structure upon determination of the secondary structures. Several examples of folding are presented. In myoglobin the heme group must be considered to reach the correct final tertiary structure. In lysozyme and phospholipase, the disulfide bondings are necessary to fasten the polypeptide chain. The selection of proper cysteine pairs among other possible ones is carried out by drawing the lampshades (locus of H atom of SH) of cysteines. In flavodoxin and thioredoxin the formation of parallel beta-structure from beta-strands is considered. The formations of antiparallel beta-structure in lysozyme and phospholipase are also discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-227X
pubmed:author
pubmed:issnType
Print
pubmed:volume
25
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-132
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Principles of protein architecture.
pubmed:affiliation
Department of Applied Physics, Waseda University, Tokyo, Japan.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't