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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.
List of contents
Microcalorimetry of Proteins and Their Complexes.- Determining the Conformational Stability of a Protein Using Urea Denaturation Curves.- Defining the Stability of Multimeric Proteins.- Protein-Protein and Ligand-Protein 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 Charge-Charge 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.
Summary
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.
Additional text
From the reviews:
"Protein Structure, Stability, and Interactions covers a thorough list of biophysical methods as applied to proteins and their environments in vivo, in vitro, and sometimes in silico. … The book begins with a tutorial on microcalorimetry by Privalov, followed by a chapter on useful protocols for urea denaturation curves … . As a whole, this book would work as a text for an advanced course in biophysical methods or as a reference book for a biophysics laboratory." (Christopher Bystroff, Journal of the American Chemical Society, Vol. 131 (23), 2009)
Report
From the reviews:
"Protein Structure, Stability, and Interactions covers a thorough list of biophysical methods as applied to proteins and their environments in vivo, in vitro, and sometimes in silico. ... The book begins with a tutorial on microcalorimetry by Privalov, followed by a chapter on useful protocols for urea denaturation curves ... . As a whole, this book would work as a text for an advanced course in biophysical methods or as a reference book for a biophysics laboratory." (Christopher Bystroff, Journal of the American Chemical Society, Vol. 131 (23), 2009)
