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Enzyme kinetics and mechanism. Part E, Energetics of enzyme catalysis /

This volume supplements Volumes 63, 64, 87, and 249 of Methods in Enzymology. These volumes provide a basic source for the quantitative interpretation of enzyme rate data and the analysis of enzyme catalysis. Among the major topics covered are Engergetic Coupling in Enzymatic Reactions, Intermediate...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Schramm, Vern L. (Editor ), Purich, Daniel L. (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: San Diego : Academic Press, �1999.
Colección:Methods in enzymology ; volume 308.
Temas:
Acceso en línea:Texto completo
Texto completo

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245 0 0 |a Enzyme kinetics and mechanism.  |n Part E,  |p Energetics of enzyme catalysis /  |c edited by Vern L. Schramm, Daniel L. Purich. 
246 3 |a Energetics of enzyme catalysis 
260 |a San Diego :  |b Academic Press,  |c �1999. 
300 |a 1 online resource (1 volume) :  |b illustrations (some color) 
336 |a text  |b txt  |2 rdacontent 
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490 1 |a Methods in enzymology ;  |v v. 308 
504 |a Includes bibliographical references and indexes. 
505 0 |a Sect. 1. Energetic coupling in enzymatic reactions -- Energetics of substate binding, catalysis, and product release -- Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase -- On the advantage of imperfect energetic linkage -- Reaction dynamics of G-protein catalyzed hydrolysis of GFP as viewed by x-ray crystallographic snapshots of Gi[alpha]₁ -- Energetics of nucleotide hydrolysis in polymer assembly/disassembly: the cases of actin and tubulin -- Fundamental mechansisms of substrate channeling -- Sect. 2. Intermediates and complexes in catalysis -- Intermediates and energetics in pyruvate phosphate dikinase -- Raman spectroscopic studies of the structures, energetics, and bond disortions of substrates bound to enzymes -- Crystallographic analysis of solvent-trapped intermediates to chymotrypsin -- Sect. 3. Detection and properties of low-barrier hydrogen bonds -- Nuclear magnetic resonance methods for the detection and study of low-barrier hydrogen bonds of enzymes -- Hydrogen bonding in enzymatic catalysis: analysis of energetic contributions -- Application of marcus rate theory to proton transfer in enzyme-catalyzed reactions -- Sect. 4. Transition state determination and inhibitors -- Enzymatic transition-state analysis and transition-state analogues -- Determining transition states from kinetic isotope effects -- Computational methods fro transition state and inhibitor recognition. 
588 0 |a Print version record. 
520 |a This volume supplements Volumes 63, 64, 87, and 249 of Methods in Enzymology. These volumes provide a basic source for the quantitative interpretation of enzyme rate data and the analysis of enzyme catalysis. Among the major topics covered are Engergetic Coupling in Enzymatic Reactions, Intermediates and Complexes in Catalysis, Detection and Properties of Low Barrier Hydrogen Bonds, Transition State Determination, and Inhibitors. The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications. 
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650 0 |a Mechanics, Analytic. 
650 0 |a Enzymology. 
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650 2 |a Kinetics  |0 (DNLM)D007700 
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650 6 |a M�ecanique analytique.  |0 (CaQQLa)201-0023814 
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650 7 |a Enzyme kinetics.  |2 fast  |0 (OCoLC)fst00913601 
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700 1 |a Schramm, Vern L.,  |e editor. 
700 1 |a Purich, Daniel L.,  |e editor. 
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