Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharolobus solfataricus | - |
- |
- |
Renatured (Comment) | Organism |
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monomeric and oligomeric enzyme show distinct behaviour on guanidine hydrochloride perturbation at neutral pH. The monomer denaturation, although complex, is reversible. Two fluorescent tryptophan classes are detectable in the monomer, monitoring the independent unfolding of two regions through a multistate transition. The oligomeric protein shows a complex denaturation pattern with the tendency to aggregate irreversibly at high denaturant concentration | Saccharolobus solfataricus |
Subunits | Comment | Organism |
---|---|---|
monomer | at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml | Saccharolobus solfataricus |
oligomer | at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml | Saccharolobus solfataricus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
at 25°C the enzyme is mostly represented by monomeric subunits at concentrations lower than 0.02 mg/ml, while oligomers are predominant at concentrations higher than 0.12 mg/ml. Only the oligomeric form is temperature resistant | Saccharolobus solfataricus |