EC Number   |
Organic Solvent |
Reference |
|---|
    5.3.1.1 | guanidine-HCl |
2.4 M, the unfolding transition is complete |
649896 |
| 5.3.1.1 | guanidine-HCl |
3.2 M, half-life of wild-type enzyme: 30 min, half-life of mutant enzyme D227N: 20 min, half-life of mutant enzyme D227A: 15 min, half-life of mutant enzyme R191S: 8 min, half-life of mutant enzyme R191A: 19 min |
651300 |
| 5.3.1.1 | guanidine-HCl |
6 M, incubation times longer thah 10 min lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme |
649746 |
| 5.3.1.1 | guanidine-HCl |
dissociation/unfolding is a highly cooperative transition in which the ternary and the secondary structures of the protein are concomitantly lost. Isolation of two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding |
650197 |
| 5.3.1.1 | urea |
8 M, incubation times longer than 5 h lead to complete unfolding. Reversible denaturation and renaturation of the homodimeric enzyme |
649746 |
| 5.3.1.1 | urea |
the enzyme is denatured in buffer with 3 M urea |
716708 |
| 5.3.1.1 | urea |
the unfolding transition midpoit is 3.5 M for Y74Cox and 5.5 M for the wild-type enzyme. The dimeric wild-type enzyme retains considerable secondary, tertiary, and quarternary structure even in 8 M urea. Urea unfolding profiles of Y74Cox in urea solution obtained by fluorescence and circular dichroism approximate a two-state transition and do not show the presence of stable intermediates over a wide range of denaturant concentrations. In wild-type enzyme the unfolding results in gradual change in spectroscopic properties |
649896 |
