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Archives of Biochemistry and Biophysics

Volumn 433, Issue 1, 2005, Pages 13-26

Enzymatic transition states: Thermodynamics, dynamics and analogue design

(1) Schramm, Vern L a

a ALBERT EINSTEIN COLLEGE OF MEDICINE (United States)

Author keywords

[No Author keywords available]

Indexed keywords

5' METHYLTHIOADENOSINE PHOSPHORYLASE; ENZYME INHIBITOR; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; ISOENZYME; PEPTIDE; PHOSPHORYLASE; PURINE NUCLEOSIDE PHOSPHORYLASE; THYMIDINE PHOSPHORYLASE; TRANSFERASE; UNCLASSIFIED DRUG;

BINDING AFFINITY; CALCULATION; CATALYSIS; CHEMICAL BOND; CHEMISTRY; CONFORMATION; CRYSTALLOGRAPHY; DISSOCIATION; DYNAMICS; ENERGY; ENZYME ACTIVITY; ENZYME STRUCTURE; HYBRID; KINETICS; MOLECULAR INTERACTION; MOTION; PRIORITY JOURNAL; PROTEIN FAMILY; SHORT SURVEY; SPECTROSCOPY; THERMODYNAMICS;

ANIMALS; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM; DRUG DESIGN; ELECTROSTATICS; ENZYME INHIBITORS; ENZYMES; HUMANS; HYDROGEN; HYDROGEN BONDING; INOSINE; KINETICS; MODELS, MOLECULAR; MOTION; PROTEIN CONFORMATION; PURINE-NUCLEOSIDE PHOSPHORYLASE; PYRIMIDINONES; PYRROLES; SUBSTRATE SPECIFICITY; THERMODYNAMICS;

EID: 9744244983 PISSN: 00039861 EISSN: None Source Type: Journal
DOI: 10.1016/j.abb.2004.08.035 Document Type: Short Survey

Times cited : (114)

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