Linked Life Data

14687947

Source:http://linkedlifedata.com/resource/pubmed/id/14687947

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-12-22
pubmed:abstractText
Studies of tryptophan fluorescence of purified influenza A virus M2 protein have identified two pH-dependent structural changes. (1) An increase in fluorescence on reduction of pH from 8 to 6 that involves tryptophan 15 within the N-terminal domain of the protein and may be associated with proton activation of the channel. (2) Quenching of the fluorescence of tryptophan 41 within the transmembrane domain of the channel by histidine 37 below pH 6 which is specifically reversed by drugs that block the M2 channel. The pH dependence of the latter effect, which monitors changes in the protonation of histidine 37, corresponds to that of proton current through the channel and provides evidence for the involvement of histidine 37 in proton permeation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0168-1702
pubmed:author
pubmed:issnType
Print
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
57-61
pubmed:dateRevised
2004-11-18
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Studies of structural changes in the M2 proton channel of influenza A virus by tryptophan fluorescence.
pubmed:affiliation
National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.
pubmed:publicationType
Journal Article