Enzymatic catalysis of the peptidyl bond rotation: Are transition state formation and enzyme dynamics directly linked?

Angewandte Chemie - International Edition

Volumn 42, Issue 5, 2003, Pages 490-492

  Fanghänel, Jörg ^a  

^a MAX PLANCK RESEARCH UNIT FOR ENZYMOLOGY OF PROTEIN FOLDING   (Germany)

Author keywords

Cyclophilin; Enzyme catalysis; Molecular dynamics; PPlase; Proteins

Indexed keywords

AMINO ACIDS; ENZYMES; ISOMERIZATION;

BOND ROTATION;

CATALYSIS;

CYCLOPHILIN;

ARTICLE; CATALYSIS; CHEMICAL BOND; ENZYME ACTIVE SITE; ENZYME SUBSTRATE COMPLEX; ISOMERISM; MOLECULAR DYNAMICS;

BINDING SITES; CATALYSIS; CYCLOPHILINS; ISOMERISM; KINETICS; MODELS, MOLECULAR; PEPTIDYLPROLYL ISOMERASE; SUBSTRATE SPECIFICITY;

EID: 0037415865     PISSN: 14337851     EISSN: None     Source Type: Journal    
DOI: 10.1002/anie.200390149     Document Type: Article

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