Linked Life Data

7537493

Source:http://linkedlifedata.com/resource/pubmed/id/7537493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-5-30
pubmed:abstractText
We have taken advantage of our previously reported high performance liquid chromatographic (HPLC) strategy to investigate the conformational behavior of the optically reversed gramicidin M (gM-), an analog of gramicidin A with all tryptophans replaced by phenylalanines, in different model membranes. It is quantitatively demonstrated for the first time that once inserted in the lipid environment, gM- (unlike the native peptide) undergoes a conformational transition from beta-helical monomers to thermodynamically stable double-stranded dimers. This transition is faster the higher the incubation temperature and can be neatly observed in both small unilamellar phospholipid vesicles and lysophospholipid micelles. The results of this study are discussed in the light of presently available data from other techniques, in the framework of the current efforts to understand structure-function relationships of linear gramicidins.
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
17
pubmed:volume
209
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
466-73
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
HPLC demonstration that an all Trp-->Phe replacement in gramicidin A results in a conformational rearrangement from beta-helical monomer to double-stranded dimer in model membranes.
pubmed:affiliation
Departament de Bioquímica i Biologia Molecular, Facultats de Ciències, Universitat de València, Burjassot, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't