Protein Structure, Stability, and Interactions
(Sprache: Englisch)
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.
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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.
Klappentext zu „Protein Structure, 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(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.
Inhaltsverzeichnis zu „Protein Structure, Stability, and Interactions “
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
Bibliographische Angaben
- 2010, X, 360 Seiten, Maße: 19,3 x 26 cm, Kartoniert (TB), Englisch
- Herausgegeben: John W. Shriver
- Verlag: Springer, Berlin
- ISBN-10: 1617378550
- ISBN-13: 9781617378553
Sprache:
Englisch
Pressezitat
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)
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