EC Number   |
Protein Variants |
Reference |
|---|
   4.6.1.24 | C196T/C603T |
double mutant to avoid restriction enzymatic scission |
680544 |
| 4.6.1.24 | D19N/D22N/E25Q/D31N/D38N/E50Q/E57Q/E76Q/D77N/D79N/E92Q/D93N |
site-directed mutagenesis using three different PCR primers |
729442 |
| 4.6.1.24 | D1W |
the mutant is studied in concentrated urea and GdnHCl solution with their disulfide bond broken, the results show that long-range effects in a denaturated protein can significantly effect the fluorescence properties |
683261 |
| 4.6.1.24 | D303N |
mutant with amino acid substitution in the binding pocket, inactive enzyme |
683904 |
| 4.6.1.24 | D31N/D38N/E92Q/D93N |
site-directed mutagenesis using two different PCR primers |
729442 |
| 4.6.1.24 | D33A |
Tm-value at pH 7.0 in Mops buffer is 16 °C lower than wild-type value. The stability of the mutant enzyme is 6 kcal/mol less than wild-type RNase Sa |
666064 |
| 4.6.1.24 | D346N |
mutant with amino acid substitution in the binding pocket |
683904 |
| 4.6.1.24 | D54A |
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate |
683260 |
| 4.6.1.24 | D54A/E60A |
mutant is modeled in silico for gaining insight into modulations of diffusional association behavior, which is reflected in the association rate |
683260 |
| 4.6.1.24 | D79A |
Tm-value at pH 7.0 in Mops buffer is 9.2 °C higher than wild-type value. The stability of the mutant enzyme is 3.3 kcal/mol less than wild-type RNase Sa |
666064 |
