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Protein Stability and Folding: A Collection of Thermodynamic Data

Autor Wolfgang Pfeil
en Limba Engleză Hardback – 11 mai 1998
The modern biosciences make many new proteins available. Nevertheless the handling of these proteins is quite difficult due to problems with their stability. This collection gives - in the form of tables - protein stability data for various temperatures and solvents. These data are most useful for the development of protein folding and the improvement of biotechnological stability for applications of proteins.
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Specificații

ISBN-13: 9783540637172
ISBN-10: 3540637176
Dimensiuni: 155 x 235 mm
Greutate: 1.12 kg
Editura: Springer Verlag
Colecția Springer
Locul publicării:Berlin, Heidelberg, Germany

Public țintă

Research

Cuprins

Introduction.- Gibbs Energy Change - Molar Values.- Enthalpy and Heat Capacity Changes - Molar Values.- Enthalpy and Heat Capacity Changes - Specific Values.- References.

Caracteristici

Erste Datensammlung (up-to-date) zur Stabilität von ProteinenAbsolut notwendig für Biochemiker, Biotechnologen, Lebensmittelwissenschaftler und Biophysiker, die mit Proteinen arbeiten

Descriere

Descriere de la o altă ediție sau format:
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 The author wishes to thank everyone who provided data, ideas, or even unpublished results.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.