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Volumn 49, Issue 29, 2010, Pages 6184-6192

The intrinsic protein flexibility of endogenous protease inhibitor TIMP-1 controls its binding interface and affects its function

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY AFFINITY; ASSOCIATION CONSTANT; BINDING CONFORMATIONS; BINDING INTERFACE; BIOLOGICAL PROCESS; CATALYTIC SITES; CLINICAL TARGETS; CONFORMATIONAL DYNAMICS; ENDOGENOUS INHIBITOR; ENTROPY COST; ENZYME CATALYSIS; HIGH RESOLUTION; HYDROGEN BOND NETWORKS; LIMITED INFORMATION; MEMBRANE TYPE-1 MATRIX METALLOPROTEINASE; METALLOPROTEINASES; MOLECULAR DYNAMICS SIMULATIONS; NOVEL PROTEINS; PROTEASE INHIBITOR; PROTEIN DYNAMICS; PROTEIN FLEXIBILITY; SINGLE-POINT MUTATION; TISSUE INHIBITOR; X-RAY STRUCTURE;

EID: 77954827231     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902141x     Document Type: Article
Times cited : (54)

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