Factors determining the relative stability of anionic tetrahedral complexes in serine protease catalysis and inhibition

Proteins: Structure, Function and Genetics

Volumn 40, Issue 1, 2000, Pages 154-167

  Shokhen, Michael ^a   Albeck, Amnon ^a  

^a BAR ILAN UNIVERSITY   (Israel)

Author keywords

Energy analysis; Enzyme mechanism; QM modeling; Transition state analogs

Indexed keywords

ACETAMIDE; ACETONE; ANION; ASPARTIC ACID; CARBOXYLIC ACID DERIVATIVE; HISTIDINE; SERINE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR;

ARTICLE; CALCULATION; CONTROLLED STUDY; COVALENT BOND; ENERGY; ENTHALPY; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; QUANTUM MECHANICS; STRUCTURE ANALYSIS; THERMODYNAMICS;

ANIONS; CATALYSIS; CATALYTIC DOMAIN; MODELS, CHEMICAL; MODELS, MOLECULAR; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; THERMODYNAMICS;

EID: 0034237219     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(20000701)40:1<154::AID-PROT170>3.0.CO;2-V     Document Type: Article

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