Linked Life Data

18283

Source:http://linkedlifedata.com/resource/pubmed/id/18283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1977-9-17
pubmed:abstractText
The binding of a series of alkyl 1-thio-beta-D-galactopyranosides to beta-D-galactosidase from E. coli has been investigated. The inhibition constants were compared to the partition coefficients for the transfer of these substrate-analogues from water to 1-octanol. The relationships between the observed binding-constants and the partition coefficients indicate that part of the aglycon group binds to a hydrophobic area that is limited in relation to the length of hydrocarbon chain that can be accomodated. Outside this area, the hydrocarbon chain is only partially desolvated. The main driving-force for binding of the aglycon group is the increase in entropy resulting from the return of water molecules from the more-organized layer around the solute molecule to the bulk-water phase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0008-6215
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
153-64
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
Binding of alkyl 1-thio-beta-D-galactopyranosides to beta-D-galactosidase from E. coli.
pubmed:publicationType
Journal Article