Energetics of enzyme catalysis
Author(s)
Bibliographic Information
Energetics of enzyme catalysis
(Methods in enzymology / editors in chief, Sidney P. Colowick, Nathan O. Kaplan, v. 308 . Enzyme kinetics and mechanism ; pt. E)
Academic Press, c1999
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Note
Includes bibliographical references and indexes
Description and Table of Contents
Description
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 in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
Table of Contents
Energetic Coupling in Enzymatic Reactions:
W.W. Cleland and D.B. Northrop, Energetics of Substrate Binding, Catalysis, and Product Release.
C.T. Grubmeyer, J.W. Gross, and M. Rajavel, Energy Coupling through Molecular Discrimination: Nicotinate Phosphoribosyltransferase.
T.S. Leyh, On the Advantages of Imperfect Energetic Linkage.
D.E. Coleman and S.R. Sprang, Reaction Dynamics of G-Protein Catalyzed Hydrolosis of GFP as Viewed by X-ray Crystallographic Snapshots of Gia1.
D.L. Purich and F.S. Southwich, Energetics of Nucleotide Hydrolysis in Polymer Assembly/Disassembly: The Cases of Actin and Tubulin.
Intermediate and Complexes in Catalysis:
K.S. Anderson, Fundamental Mechanisms of Substrate Channeling.
D. Dunnaway-Mariano, Intermediates and Energetics in Pyruvate Phosphate Dikinase.
H. Deng and R. Callender, Raman Spectroscopic Studies of the Structures, Energetics, and Bond Distortions of Substrates Bound to Enzymes.
G.K. Farber, Crystallographic Analysis of Solvent-Trapped Intermediates of Chymotrypsin.
Detection and Properties of Low-Barrier Hydrogen Bonds:
A.S. Mildvan, T.K. Harris, and C. Abeygunawardana, NMR Methods for the Detection and Study of Low-Barrier Hydrogen Bonds of Enzymes.
S. Shan and D. Herschlag, Hydrogen Bonding in Enzymatic Catalysis: Analysis of Energetic Contributions.
A.J. Kresge and D.N. Silverman, Application of Marcus Rate Theory to Proton Transfer in Enzyme-Catalyzed Reactions.
Transition State Determination and Inhibitors:
V.L. Schramm, Enzymatic Transition State Analysis and Transition State Analogues.
P.J. Berti, Determinin Transition States from Kinetic Isotope Effects.
B.B. Braunheim and S.D. Schwartz, Computational Methods for Transition State and Inhibitor Recognition.
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