Protein Stability and Folding: Supplement 1 A Collection of Thermodynamic Data
Autor Wolfgang Pfeilen Limba Engleză Paperback – 2 oct 2013
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Specificații
ISBN-13: 9783662128404
ISBN-10: 3662128403
Pagini: 536
Ilustrații: XIII, 521 p. 1 illus.
Dimensiuni: 210 x 279 x 28 mm
Greutate: 1.19 kg
Ediția:Softcover reprint of the original 1st ed. 2001
Editura: Springer Berlin, Heidelberg
Colecția Springer
Locul publicării:Berlin, Heidelberg, Germany
ISBN-10: 3662128403
Pagini: 536
Ilustrații: XIII, 521 p. 1 illus.
Dimensiuni: 210 x 279 x 28 mm
Greutate: 1.19 kg
Ediția:Softcover reprint of the original 1st ed. 2001
Editura: Springer Berlin, Heidelberg
Colecția Springer
Locul publicării:Berlin, Heidelberg, Germany
Public țintă
ResearchDescriere
In 1998, we published the data compilation PROTEIN STABILITY AND FOLDING which covered the data from the early beginnings of thermodynamic studies of protein folding until 1996. Since then, the amount of available thermodynamic data has increased nearly twice. The data constitute very important additions to the information on the protein folding problem, the construction of mutant protein, and the practical application of proteins in various fields. The Supplement covers the period 1997-1999 and is designed to make the vast amount of present data accessible to multidisciplinary research where chemistry, physics, biology, and medicine are involved and also biotechnology, pharmaceutical and food research. At the same time the data could be helpful to identify problems unsolved so far, and to avoid unnecessary duplication of scientific work. The structure of the Supplement is the same as in the previous data compilation. However, some additional data characterizing protein-denaturant interaction and protein unfolding by trifluoroethanol have been added. In that context, some previous data have been reconsidered. The author wishes to thank everyone who provided data, ideas, or even unpublished results. Furthermore, support by the Deutsche Forschungsgemeinschaft (INK 16 BI-I) is gratefully acknowledged. Finally, I would like to thank the staff of Springer Verlag for their efforts and for excellent assistance during the production of the data collections.
Cuprins
Table 1: Gibbs energy change — molar values.- Table 2: Enthalpy and heat capacity changes — molar values.- Table 3: Enthalpy and heat capacity changes — specific values.- Table 4: Protein denaturation by trifluoroethanol (TFE) and other alcohol-based cosolvents.- References (Table 1–4).- Index of Proteins.
Caracteristici
The set includes the first edition plus the supplement 1 thus giving the up-to-date relevant data for the stability of proteins
Absolutely useful for biochemists, biotechnologists, food scientists and biophysisists working with proteins
Absolutely useful for biochemists, biotechnologists, food scientists and biophysisists working with proteins