
Protein Stability and Folding
A Collection of Thermodynamic Data
Wolfgang Pfeil(Author)
Springer (Publisher)
Published on 16. October 2012
Book
Paperback/Softback
XIII, 658 pages
978-3-642-63716-2 (ISBN)
Description
Protein folding remains one of the most exclusive problems of modern biochemistry. Structure analysis has given access to the wealth of the molecular architecture of pro teins. As architecture needs static calculations, protein structure is always related to thermodynamic factors that govern folding and stability of a particular folded protein over the non-organized polypeptide chain. During the past decades a huge amount of thermodynamic data related to protein folding and stability has been accumulated. The data are certainly of importance in dechiffring the protein folding problem. At the same time, the data can guide the con struction of modified and newly synthesized proteins with properties optimized for particular application. The intention of this book is a generation of a data collection which makes the vast amount of present data accessible for multidisciplinary research where chemistry, phy sics, biology, and medicine are involved and also pharmaceutical and food research and technology. It took several years to compile all the data and the author wishes to thank everyone who provided data, ideas or even unpublished results. The author is, in particular, indebted to Prof. Wadso (Lund, Sweden) and IUPAC's Steering Committee on Bio physical Chemistry. Furthermore, support by the Deutsche Forschungsgemeinschafi (INK 16 AI-I) is acknowledged.
More details
Edition
Softcover reprint of the original 1st ed. 1998
Language
English
Place of publication
Berlin
Germany
Publishing group
Springer Berlin
Target group
Professional and scholarly
Research
Illustrations
XIII, 658 p.
Dimensions
Height: 235 mm
Width: 155 mm
Thickness: 37 mm
Weight
1007 gr
ISBN-13
978-3-642-63716-2 (9783642637162)
DOI
10.1007/978-3-642-58760-3
Schweitzer Classification
Other editions
Additional editions

Book
1998
Springer
€213.95
Article exhausted; check different version
Content
1 Evaluation of the approaches for the determination of conformational stability and related thermodynamic quantities.- 2 Comments on the tabulated data.- 3 Why to prefer complex thermodynamic functions.- References.- Table 1. Gibbs energy change-molarvalues.- Table 2. Enthalpy and heat capacity changes-molar values.- Table 3. Enthalpy and heat capacity changes-specific values.- References (Tables 1-3).- Index of Proteins.