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pubmed-article:11078193pubmed:abstractTextIsothermal 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.lld:pubmed
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pubmed-article:11078193pubmed:articleTitleStereoselective binding of an enantiomeric pair of stromelysin-1 inhibitors caused by conformational entropy factors.lld:pubmed
pubmed-article:11078193pubmed:affiliationUniversity of Alabama at Birmingham, 35294, USA. matthew_parker@vpharm.comlld:pubmed
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