Essential publication for researchers in all fields of life sciences. Key Features * Major topics covered include: * Deciphering rules of helix stability in peptides * Protein Folding in Membranes * Molecular Crowding * Study of the Bohr Effect in Hemoglobin Intermediates * Photoacoustic Calorimetry of Proteins * Theoretical Aspects of Isothermal Titration Calorimetry * Energetic Methods to Study Bifunctional Biotin Repressor.

General Description of the Volume: The very existence of biological structures and their functional interactions are dictated by energetic relationships. Thus the central theme of this volume is that thermodynamic methods, i.e. techniques that probe the energetics of biological macromolecules, now comprise a powerful and practical family of tools for research in modern biology. The application of thermodynamics and statistical thermodynamics to biochemical and biophysical systems is presented. This volume supplements Methods in Enzymology, Volume 259. General Description of the Series: 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. Key Features * Major topics covered include: * Deciphering rules of helix stability in peptides * Protein Folding in Membranes * Molecular Crowding * Study of the Bohr Effect in Hemoglobin Intermediates * Photoacoustic Calorimetry of Proteins * Theoretical Aspects of Isothermal Titration Calorimetry * Energetic Methods to Study Bifunctional Biotin Repressor

Volume 323 of Methods in Enzymology is dedicated to the energetics of biological macromolecules. Understanding the molecular mechanisms underlying a biological process requires detailed knowledge of the structural relationships within the system and an equally detailed understanding of the energetic driving forces that control the structural interactions. This volume presents modern thermodynamic techniques currently being utilized to study the energetic driving forces in biological systems. It will be a useful reference source and textbook for scientists and students whose goal is to understand the energetic relationships between macromoleculer structures and biological functions. This volume supplements Volumes 259 and Volume 295 of Methods in Enzymology. Key Features * Probing Stability of Helical Transmembrane Proteins * Energetics of Vinca Alkaloid Interactions with Tubulin * Deriving Complex Ligand Binding Formulas * Mathematical Modeling of Cooperative Interactions in Hemoglobin * Analysis of Interactions of Regulatory Protein TyrR with DNA * Parsing Free Energy of Drug-DNA Interactions * Use of Fluorescence as Thermodynamics Tool

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

Energetics of Biological Macromolecules, Part E focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, spectroscopic methods and quantitative analysis as well as on cooperativity in protein folding. NMR and mass spectrometry methods are discussed. Allosteric Enzymes and Receptors Cooperativity in Protein Folding and Assembly