EC Number   |
Protein Variants |
Reference |
|---|
   3.1.31.1 | A128S |
single point mutation in D21N/T33V/T41I/S59A/P117G/A128A, designed to study inductive effects and longer-range interactions between elements of the network, pKa values of histidines (His8, His46, His121, His124) are obtained by analysis of the pH titration monitored through the 1 H chemical shifts of the C(epsilon) H resonance of each histidine (NMR spectroscopy) |
699534 |
| 3.1.31.1 | A1C/Q149C |
SNase double mutant, N- and C-terminal residues replaced by cysteine, constructed from the plasmid (pMT7-SN) of wild-type SNase using the Kunkel method, can form disulfide bond |
696005 |
| 3.1.31.1 | A90S |
pH-value, at which the acid-denaturation is half completed is 4.19, compared to pH 3.76 for wild-type enzyme. The apparent number of protons which trigger the denaturation and are taken up by the protein upon denaturation is 1.0 for the mutant enzyme compared to 1.8 for wild-type enzyme |
664352 |
| 3.1.31.1 | D143G |
Tm value for mutant enzyme is 50.53°C, compared to 50.98°C for wild-type enzyme |
664893 |
| 3.1.31.1 | D143K |
charge reversal |
657950 |
| 3.1.31.1 | D143N |
charge reversal |
657950 |
| 3.1.31.1 | D146G |
Tm value for mutant enzyme is 50.99°C, compared to 50.98°C for wild-type enzyme |
664893 |
| 3.1.31.1 | D19G |
Tm value for mutant enzyme is 52.06°C, compared to 50.98°C for wild-type enzyme |
664893 |
| 3.1.31.1 | D19K |
charge reversal |
657950 |
| 3.1.31.1 | D19L |
charge reversal |
657950 |
