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. - Spectroscopic Detection of Reaction Intermediates - Isotopic and Kenetic Detection of Reaction Intermediates - Chemical Trapping and Inhibitor Methods for Detecting Reaction Intermediates

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.

The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. This volume presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions. - Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules - Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research - Offers step-by-step lab instructions, including necessary equipment, from a global research community

This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed.*Methods for Evaluating Cooperativity in a Dimeric Hemoglobin*Multiple-Binding of Ligands to a Linear Biopolymer*Fluorescence Quenching Methods to Study Protein-Nucleic Acid Interactions*Linked Equilibria in Biotin Repressor Function: Thermodynamic, Structural and Kinetic Analysis

Far more than a comprehensive treatise on initial-rate and fast-reaction kinetics, this one-of-a-kind desk reference places enzyme science in the fuller context of the organic, inorganic, and physical chemical processes occurring within enzyme active sites. Drawing on 2600 references, Enzyme Kinetics: Catalysis & Control develops all the kinetic tools needed to define enzyme catalysis, spanning the entire spectrum (from the basics of chemical kinetics and practical advice on rate measurement, to the very latest work on single-molecule kinetics and mechanoenzyme force generation), while also focusing on the persuasive power of kinetic isotope effects, the design of high-potency drugs, and the behavior of regulatory enzymes. - Historical analysis of kinetic principles including advanced enzyme science - Provides both theoretical and practical measurements tools - Coverage of single molecular kinetics - Examination of force generation mechanisms - Discussion of organic and inorganic enzyme reactions

Practical Enzyme Kinetics provides a practical how-to guide for beginning students, technicians, and non-specialists for evaluating enzyme kinetics using common software packages to perform easy enzymatic analyses.

The aim of Numerical Computer Methods, Part D is to brief researchers of the importance of data analysis in enzymology, and of the modern methods that have developed concomitantly with computer hardware. It is also to validate researchers' computer programs with real and synthetic data to ascertain that the results produced are what they expected. Selected Contents: Prediction of protein structure Modeling and studying proteins with molecular dynamics Statistical error in isothermal titration calorimetry Analysis of circular dichroism data Model comparison methods