Linked Life Data

2458135

Source:http://linkedlifedata.com/resource/pubmed/id/2458135

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-10-25
pubmed:abstractText
Using [15N-Val7]gramicidin A it is shown by solid state 15N-NMR that in dimyristoylphosphatidylcholine model membrane preparations evidence is obtained for two different backbone conformations of gramicidin. One of these conformations is the familiar channel state while a second conformation possesses very different dynamic and structural characteristics. The relative amounts of the conformations depend upon the solvent used to initially codissolve peptide and lipid. Furthermore, by incubation of the samples at modestly elevated temperatures a conversion can be induced from the non-channel to the channel state in a lipid environment.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
943
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
535-40
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Solid-state 15N-NMR evidence that gramicidin A can adopt two different backbone conformations in dimyristoylphosphatidylcholine model membrane preparations.
pubmed:affiliation
Department of Chemistry, Florida State University, Tallahassee.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't