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Protein Structure, Stability, and Interactions

Handbook / Manual

Series: Methods in Molecular Biology Volume: 490

Edited By: John M Walker

372 pages, Illustrations

Humana Press

Hardback | Nov 2008 | #179593 | ISBN-13: 9781588299543
Availability: Usually dispatched within 1-2 weeks Details
NHBS Price: £108.00 $141/€123 approx

About this book

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.

It 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.

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)


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 Jorg Rosgen 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

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