Linked Life Data

2759832

Source:http://linkedlifedata.com/resource/pubmed/id/2759832

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-9-8
pubmed:abstractText
A new method is elaborated for determining the hydropathy profile of membrane haemoproteins. The method is called membrane propensity for haemoproteins (MPH) and is based on the statistical analysis of the amino acid composition of the predicted transmembrane regions of cytochrome b from the bc1 and the b6f complexes. The accuracy of the MPH method in predicting the ends of the known transmembrane segments of the reaction center of Rhodopseudomonas viridis is higher than that obtained by hydropathy methods based on physico-chemical parameters. The MPH method is able to clearly exclude from the membrane polypeptides that are not consistently predicted to be transmembrane by other methods or techniques, for instance the region corresponding to helix IV of mitochondrial cytochrome b. A correlation has been found between the shape of the hydropathy profile of the transmembrane segments predicted by this new method and the known structure of the membrane-spanning helices of Rhodobacter reaction centers. From the above correlation it is proposed that the haem-coordinating domain of mitochondrial cytochrome b is folded in a novel structure, called "clepsydra domain", which is formed by distorted transmembrane helices packed in a waisted antiparallel bundle.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0021-2938
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1-22
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:articleTitle
New approaches to the prediction of the folding of membrane proteins with redox function.
pubmed:affiliation
Dipartimento di Biologia, Università di Bologna.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't