Protein Stability and Folding Supplement 1: A Collection of Thermodynamic Data.

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Springer Science & Business Media, 2001 - Science - 521 pages
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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. The first supplement contains material covering 1997-1999. Some previous data have also been included into the present work. Previous papers on denaturant-induced protein unfolding have been reconsidered to include additional parameters. Furthermore, data on TFE-induced unfolding have been arranged in a new Table. Finally, some data have been added which slipped through during the preparation of the data collection.
 

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Contents

References
5
Table 1 Gibbs Energy Change Molar Values
7
Table 2 Enthalpy and Heat Capacity Changes Molar Values
283
Table 3 Enthalpy and Heat Capacity Changes Specific Values
451
Tab1e 4 Protein Denaturation by Trif1uoroethanol TFE and Other A1coho1Based Cosolvents
461
References and Index of Proteins
473
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Page 498 - Winkler, JR, and Gray, HB (1999) Cytochrome b562 folding triggered by electron transfer: approaching the speed limit for formation of a four-helix-bundle protein [in process citation]. Proc. Natl Acad. Sci., USA, 96,6587.
Page 495 - Chaudhuri, TK, Horii, K., Yoda, T., Arai, M., Nagata, S., Terada, TP, Uchiyama, H., Ikura, T., Tsumoto, K., Kataoka, H., Matsushima, M., Kuwajima, K., amd Kumagai, I.
Page 495 - CHITI F., TADDEI N., WHITE PM, BUCCIANTINI M., MAGHERINI F., STEFANI M.

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