Linked Life Data

7730381

Source:http://linkedlifedata.com/resource/pubmed/id/7730381

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1995-6-1
pubmed:abstractText
A new theoretical method for free energy calculations is used to compute the absolute binding constants for beta-D-glucose and methyl-beta-D-galactoside to the periplasmic glucose/galactose receptor from Salmonella typhimurium. The computer simulation results agree well with available experimental data and make it possible to assess the sources of both the high affinity as well as the specificity for glucose. It was found that the major contribution to the binding energy comes from electrostatic interactions and particularly hydrogen bonds of the charge-dipole type. We also predict the structure of the complex with methyl-galactoside as this has not yet been experimentally determined.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
270
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9978-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Sugar recognition by a glucose/galactose receptor. Evaluation of binding energetics from molecular dynamics simulations.
pubmed:affiliation
Department of Molecular Biology, Uppsala Biomedical Centre, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't