Linked Life Data

9050155

Source:http://linkedlifedata.com/resource/pubmed/id/9050155

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1997-6-13
pubmed:abstractText
Hydrogen exchange experiments for a membrane-bound polypeptide could lead to interesting functional and structural insights. Here, hydrogen/deuterium exchange, saturation transfer and differential relaxation experiments have been performed on oriented lipid bilayer-bound polypeptide samples to measure the exchange lifetimes. The polypeptide, gramicidin A, forms a monovalent cation selective channel across membranes. The pH dependent results suggest that the indole N epsilon 1-H groups show base catalyzed hydrogen exchange, but that the backbone amide sites are not base catalyzed, consistent with the exclusion of anions from this channel. Furthermore, the recently described [1] orientational distribution of the individual peptide carbonyls (i.e. carbonyls either tipped slightly in toward or away from the channel axis) is consistent with the observed difference in odd- and even-numbered amide residue exchange lifetimes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0926-2040
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
177-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Hydrogen exchange in the lipid bilayer-bound gramicidin channel.
pubmed:affiliation
Department of Chemistry, Florida State University, Tallahassee 32306-4005, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.