Supporting and up-dating previous volumes, this text focuses on theory and practical applications for both established methods and new procedures. The volume presents an overview of many techniques currently used to study protein stability and interactions.

In the areas of biochemistry and cell biology, characterizations of stability and molecular interactions call for a quantitative approach with a level of precision that matches the fine tuning of these interactions in a living cell. Supporting and up-dating previous Methods in Molecular Biology ™ volumes, Protein Structure, Stability, and Interactions approaches its subject with a focus on theory and practical applications for both established methods as well as exciting new procedures. The volume presents an overview of many techniques currently used to study protein stability and interactions, including scanning and titration calorimetry, spectroscopic methods, high field NMR, and analytical ultracentrifugation. As a volume of the highly successful Methods in Molecular Biology ™ series, this work provides the kind of detailed description and implementation advice that is crucial for getting optimal results.

Cutting-edge and easy to reference, Protein Structure, Stability, and Interactions is an ideal guide for all scientists interested in biomolecular interactions.

A comprehensive guide to measuring biomolecular interactions for new as well as established investigators Includes overviews of methods along with details to assist first time users Covers the necessary theory for analyzing a wide array of different kinds of binding data Contains descriptions of methods for studying both intermolecular and intramolecular interactions Includes methods for describing interactions in vivo including the effects of solvent and crowding

Inhalt
Microcalorimetry of Proteins and Their Complexes.- Determining the Conformational Stability of a Protein Using Urea Denaturation Curves.- Defining the Stability of Multimeric Proteins.- ProteinProtein and LigandProtein Interactions Studied by Analytical Ultracentrifugation.- Monitoring Molecular Interactions by NMR.- Ligand-Binding Interactions and Stability.- A Method for Direct Measurement of Protein Stability In Vivo.- Quantifying the Roles of Water and Solutes (Denaturants, Osmolytes, and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Model.- Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions.- Defining the Role of Salt Bridges in Protein Stability.- Protein Stabilization by the Rational Design of Surface ChargeCharge Interactions.- NMR Analysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange.- Single-Molecule Fluorescence Studies of Protein Folding.- Experimental Characterization of the Denatured State Ensemble of Proteins.