Protein Stability and Folding Theory and Practice

About this book

In Protein Stability and Folding: Theory and Practice, world-class scientists present in a single volume a comprehensive selection of hands-on recipes for all of the major techniques needed to understand the conformational stability of proteins, as well as their three-dimensional folding. The distinguished contributors provide clear, step-by-step instructions along with many troubleshooting tips, alternative procedures, and informative explanations about why certain steps are necessary. Even highly skilled researchers will find many time-saving methods. Among the techniques discussed are fluorescent, ultraviolet, and infrared spectroscopy; HPLC peptide mapping; differential scanning calorimetry; and hydrogen exchange. Shirley's Protein Stability and Folding: Theory and Practice will ensure a significant difference in the outcome of your experiments, producing the result desired even for beginners.

Contents

Noncovalent Forces Important to the Conformational Stability of Protein Structures. Degradative Covalent Reactions Important to Protein Stability Fluorescence Spectroscopy. Ultraviolet Absorption Spectroscopy. Circular Dichroism. Infrared Spectroscopy. Identifying Sites of Posttranslational Modifications in Proteins via HPLC Peptide Mapping. Urea and Guanidine Hydrochloride Denaturation Curves. Differential Scanning Calorimetry. Disulfide Bonds in Protein Folding and Stability. Solvent Stabilization of Protein Structure. Site-Directed Mutagenesis to Study Protein Folding and Stability. Hydrogen Exchange Techniques. Protein Folding Kinetics. Molten Globules. Chaperonin-Assisted Protein Folding of the Enzyme Rhodanese by GroEL/GroES. Index.

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