Protein Stability and Folding Supplement 1: A Collection of Thermodynamic Data.
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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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
Tab1e 4 Protein Denaturation by Trif1uoroethanol TFE and Other A1coho1Based Cosolvents
References and Index of Proteins
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Protein Stability and Folding: Supplement 1 A Collection of Thermodynamic Data
No preview available - 2014
50 mM sodium absence absorption amino acid Appr./Rem Approach Approach/Remarks Ref trs Approach/Remarks Ref wild average Bacillus binding buffer calculated coli contains continued curve Cytochrome data from Ref deconvolution denaturation derived dimer domain double mutant EDTA exchange far-UV CD folding fragment glycine GuHCI GuHCl heat human intermediate kinetics kJ/mol kJ/mol/K LEM-SB linear extrapolation lysozyme measured in 50 monitored by CD monitored by far-UV monitored by fluorescence Mutant pH mutants Mutant pH N-terminal NaCl native obtained oxidized peptide pH T AG pH T trs phosphate buffer position potassium phosphate presence pressure Protein pH Recombinant reduced Ref wild type reference Remarks repressor residues RNase sodium acetate sodium phosphate stability Table temperature trans transition monitored Transition pH treatment Tris-HCl two-state type and mutants unfolding urea variant varying wild type 7.0 ΔΗ
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.