Protein Stability and Folding

Theory and Practice

AvBret A. Shirley,Bret A. Shirley

Häftad, Engelska, 1995

Del i serien Methods in Molecular Biology

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Beskrivning

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.

Produktinformation

Utgivningsdatum:1995-03-24
Mått:155 x 235 x 24 mm
Vikt:658 g
Format:Häftad
Språk:Engelska
Serie:Methods in Molecular Biology
Antal sidor:377
Upplaga:1995
Förlag:Humana Press Inc.
ISBN:9780896033016

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Recensioner i media

...very useful for any biochemist who needs to understand concepts of protein folding and stability and how protein folding can be monitored and studied. This is a good book for student researchers and should be considered as an addition to courses on protein structure.-Doody's Health Sciences Book Review Journal

Innehållsförteckning

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.