|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
21
|
|
pubmed:dateCreated |
2001-2-7
|
|
pubmed:abstractText |
Isothermal titration calorimetry was used to analyze the binding of an enantiomeric pair of inhibitors to the stromelysin-1 catalytic domain. Differences in binding affinity are attributable to different conformational entropy penalties suffered upon binding. Two possible explanations for these differences are proposed.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Nov
|
|
pubmed:issn |
0960-894X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
6
|
|
pubmed:volume |
10
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2427-30
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:11078193-Calorimetry,
pubmed-meshheading:11078193-Catalytic Domain,
pubmed-meshheading:11078193-Humans,
pubmed-meshheading:11078193-Hydroxamic Acids,
pubmed-meshheading:11078193-Matrix Metalloproteinase 3,
pubmed-meshheading:11078193-Molecular Conformation,
pubmed-meshheading:11078193-Molecular Structure,
pubmed-meshheading:11078193-Oligopeptides,
pubmed-meshheading:11078193-Protease Inhibitors,
pubmed-meshheading:11078193-Protein Binding,
pubmed-meshheading:11078193-Stereoisomerism,
pubmed-meshheading:11078193-Thermodynamics
|
|
pubmed:year |
2000
|
|
pubmed:articleTitle |
Stereoselective binding of an enantiomeric pair of stromelysin-1 inhibitors caused by conformational entropy factors.
|
|
pubmed:affiliation |
University of Alabama at Birmingham, 35294, USA. matthew_parker@vpharm.com
|
|
pubmed:publicationType |
Journal Article
|
