Linked Life Data

7690593

Source:http://linkedlifedata.com/resource/pubmed/id/7690593

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
37
pubmed:dateCreated
1993-10-20
pubmed:abstractText
The interaction of the voltage-dependent channel-forming peptide alamethicin with dioleoylphosphatidylcholine (DOPC) small unilamellar vesicles (SUV) has been studied using circular dichroism spectroscopy over a range of wavelengths and temperatures. Evidence is presented for the existence of two distinct membrane-bound states of the peptide which reflect different extents of peptide-peptide interaction. An elevated temperature is found to diminish the apparent peptide-peptide interaction. These results provide insight into the general problem of helix-helix interaction in membranes and provide experimental support for the proposal [Popot, J. L., & Engelman, D. M. (1990) Biochemistry 29, 4031-4037] that these interactions can be enthalpically favorable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9819-25
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Temperature dependence of the interaction of alamethicin helices in membranes.
pubmed:affiliation
Department of Crystallography, Birkbeck College, University of London, U.K.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't