The Observed Change in Heat Capacity Accompanying the Thermal Unfolding of Proteins Depends on the Composition of the Solution and on the Method Employed To Change the Temperature of Unfolding
| Autor: | Yufeng Liu, Julian M. Sturtevant |
|---|---|
| Rok vydání: | 1996 |
| Předmět: |
Protein Denaturation
Protein Folding Sucrose Hot Temperature Equilibrium unfolding Glycine Thermodynamics Buffers Guanidines Biochemistry Heat capacity chemistry.chemical_compound Differential scanning calorimetry Thermal Ribonuclease skin and connective tissue diseases Guanidine Calorimetry Differential Scanning biology Chemistry Ribonuclease Pancreatic Solutions Crystallography biology.protein Muramidase Composition (visual arts) sense organs Lysozyme |
| Zdroj: | Biochemistry. 35:3059-3062 |
| ISSN: | 1520-4995 0006-2960 |
| DOI: | 10.1021/bi952198j |
| Popis: | The apparent change in heat capacity, delta C(p), accompanying the thermally induced unfolding of lysozyme and of ribonuclease A was determined by means of differential scanning calorimetry in dilute aqueous buffer containing one of the following added solutes: 0.5 M or 1.0 M sucrose, 1.0 M glycine, 0.5 M, 1.0 M, or 2.0 M guanidinium chloride, 10% glycerol, or 0.5 M NaCl over a pH range. In each system the temperature of half-completion, t1/2, of the unfolding transition was varied by varying the pH. The resulting enthalpies of denaturation were linearly dependent on t1/2 for each solvent system. The resulting values of delta C(p) for each protein showed variation of almost 2-fold. Such large variations in the sensitivity of the proteins to temperature changes are not readily interpreted. |
| Databáze: | OpenAIRE |
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