A Collection of Thermodynamic Data
Buch, Englisch, 658 Seiten, Format (B × H): 155 mm x 235 mm, Gewicht: 1007 g
ISBN: 978-3-642-63716-2
Verlag: Springer
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It took several years to compile all the data and the author wishes to thank everyone who provided data, ideas or even unpublished results.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.
Zielgruppe
Research
Autoren/Hrsg.
Fachgebiete
- Technische Wissenschaften Verfahrenstechnik | Chemieingenieurwesen | Biotechnologie Lebensmitteltechnologie und Getränketechnologie
- Naturwissenschaften Physik Angewandte Physik Biophysik
- Naturwissenschaften Biowissenschaften Biochemie (nichtmedizinisch)
- Medizin | Veterinärmedizin Medizin | Public Health | Pharmazie | Zahnmedizin Pharmazie
- Technische Wissenschaften Verfahrenstechnik | Chemieingenieurwesen | Biotechnologie Biotechnologie
Weitere Infos & Material
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.
