Linked Life Data

8639562

Source:http://linkedlifedata.com/resource/pubmed/id/8639562

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
20
pubmed:dateCreated
1996-7-15
pubmed:abstractText
The peptide alamethicin forms channels with a variety of conductance states. Selective stabilization of a particular state should simplify the task of understanding conductance in terms of channel structure. We synthesized two different covalent dimers of alamethicin in which peptides were linked at their C-terminal ends by flexible tethers. Both dimeric peptides formed channels with conductances that matched those of alamethicin channels. Particular conductance states were selectively stabilized, however, with lifetimes up to 170-fold longer than the same states observed with monomers. In addition, tethering appeared to limit the size of the structures formed so that, even at higher peptide concentrations, a single predominant conductance state was obtained. We suggest this state corresponds to a channel made from six alamethicin molecules (three dimers).
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6225-32
pubmed:dateRevised
2009-9-29
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Engineering stabilized ion channels: covalent dimers of alamethicin.
pubmed:affiliation
Department of Chemistry, University of Toronto, Canada.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't