1 Microcalorimetry of Proteins and Their Complexes Peter L. Privalov 2 Determining the Conformational Stability of a Protein Using Urea Denaturation Curves Kevin L. Shaw, J. Martin Scholtz, C. Nick Pace, and G. R. Grimsley 3 Defining the Stability of Multimeric Proteins John W. Shriver and Stephen P. Edmondson 4 Protein-Protein and Ligand-Protein Interactions Studied by Analytical Ultracentrifugation Walter Stafford 5 Monitoring Molecular Interactions by NMR James M. Lipchock and J. Patrick Loria 6 Ligand Binding Interactions and Stability John W. Shriver and Stephen P. Edmondson 7 A Method for Direct Measurement of Protein Stability in Vivo Zoya Ignatova and Lila Gierasch 8 Quantifying the Roles of Water and Solutes (Denaturants, Osmolytes, and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Model Laurel M. Pegram and M. Thomas Record, Jr. 9 Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions Jörg Rösgen 10 Defining the Role of Salt Bridges in Protein Stability Ilian Jelesarov and Andrey Karshikoff 11 Protein Stabilization by the Rational Design of Surface Charge-Charge Interactions Katrina L. Schweiker and George I. Makhatakze 12 Analysis of Native State Protein Conformational Flexibility by Hydrogen Exchange Griselda Hernandez and David M. LeMaster 13 Single-Molecule Fluorescence Studies of Protein Folding G. Ulrich Nienhaus 14 Experimental Characterization of the Denatured State Ensemble of Proteins Jae-Hyun Cho and Dan Raleigh
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(TM) 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(TM) 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