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Literature summary for 2.7.2.3 extracted from
- Thermodynamic analysis of the nondenaturational conformational change of bakers yeast phosphoglycerate kinase at 24°C (2008), Arch. Biochem. Biophys., 478, 206-211.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 24 | - |
two stable, folded conformers with an abrupt conformational transition occurring at 24°C. The transition state thermodynamics for the low- to high-temperature conformational change are calculated from slow-scan-rate differential scanning calorimetry measurements where it is found that the free energy barrier for the conversion is 90 kJ/mol and the transition state possesses a significant unfolding quality | Saccharomyces cerevisiae |
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