Elucidating the origin of long residence time binding for inhibitors of the metalloprotease thermolysin

ACS Chemical Biology

Volumn 12, Issue 1, 2017, Pages 225-233

  Cramer, Jonathan ^a   Krimmer, Stefan G ^a   Fridh, Veronica ^b   Wulsdorf, Tobias ^a   Karlsson, Robert ^b   Heine, Andreas ^a   Klebe, Gerhard ^a  

^a PHILIPPS UNIVERSITY MARBURG   (Germany)

^b GE Healthcare Bio Sciences AB   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

METALLOPROTEINASE INHIBITOR; THERMOLYSIN; ASPARTIC ACID; DIPEPTIDE; ENZYME INHIBITOR; ORGANOPHOSPHORUS COMPOUND;

ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DISSOCIATION CONSTANT; DISSOCIATION RATE CONSTANT; ENZYME BINDING; HYDROGEN BOND; IONIC STRENGTH; KINETIC PARAMETERS; PRIORITY JOURNAL; PROTEIN CONFORMATION; SURFACE PLASMON RESONANCE; X RAY CRYSTALLOGRAPHY; ANTAGONISTS AND INHIBITORS; CHEMICAL MODEL; CHEMISTRY; CONFORMATION; KINETICS; SYNTHESIS; TIME FACTOR;

ASPARTIC ACID; CRYSTALLOGRAPHY, X-RAY; DIPEPTIDES; ENZYME INHIBITORS; HYDROGEN BONDING; KINETICS; MODELS, CHEMICAL; MOLECULAR CONFORMATION; ORGANOPHOSPHORUS COMPOUNDS; THERMOLYSIN; TIME FACTORS;

EID: 85019607617     PISSN: 15548929     EISSN: 15548937     Source Type: Journal    
DOI: 10.1021/acschembio.6b00979     Document Type: Article

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