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

• Άλλοι συγγραφείς: Schramm, Vern L. (Επιμελητής έκδοσης), Purich, Daniel L. (Επιμελητής έκδοσης)
• Μορφή: Ηλ. βιβλίο
• Γλώσσα: English
• Έκδοση: San Diego : Academic Press, ©1999.
• Σειρά: Methods in enzymology ; volume 308.
• Θέματα: Enzyme kinetics.; Enzymes > Metabolism.; Mechanics, Analytic.; Enzymes > metabolism.; Kinetics.; Cinétique enzymatique.; Enzymologie.; SCIENCE > Life Sciences > Biochemistry.; Electronic books.

Πίνακας περιεχομένων:

• 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.