Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
2001-6-20
pubmed:abstractText
Substrate transport through the membrane protein maltoporin is facilitated by an affinity site in the channel. The analysis of the ion current fluctuations induced by penetration of the sugar into the channel yields the kinetic constants. Modification of the affinity site by replacing the aromatic residues suggests that nature has optimized the channel protein for maximum affinity at the extracellular side, as well as for an increased off-rate to eject a sugar trapped in the pore towards the periplasmic side.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0031-9007
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
86
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5624-7
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Facilitated substrate transport through membrane proteins.
pubmed:affiliation
Institut de Pharmacologie et de Biologie Structurale, CNRS-UMR 5089, Université P. Sabatier, 205 route de Narbonne, 31077 Toulouse, France.
pubmed:publicationType
Journal Article