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Literature summary for 4.2.1.1 extracted from
- Thermodynamic analysis of the low- to physiological-temperature nondenaturational conformational change of bovine carbonic anhydrase (2007), J. Biochem. Mol. Biol., 40, 205-211.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| erythrocyte | - |
Bos taurus | - |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
the enzyme possesses two stable folded conformers with the conformational transition occurring at about 30°C. The methodology yields a stability curve for the complete unfolding of the enzyme below this temperature but only the partial unfolding, to the molten globule state, above it. The transition state thermodynamics for the low-term to physiological-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/mole and the transition state possesses a substantial unfolding quality | Bos taurus |
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