EC Number   |
General Stability |
Reference |
|---|
   3.1.26.4 | calculation of stability versus hydrophobicity and residue contacts |
657146 |
| 3.1.26.4 | denaturation kinetics, midpoint at about 1.6 M urea and 5°C |
664911 |
| 3.1.26.4 | denaturation kinetics, midpoint at about 1.8 M urea and 5°C |
664911 |
| 3.1.26.4 | metal binding stabilizes the enzyme by decreasing its unfolding rate, mechanism |
657310 |
| 3.1.26.4 | metal ion and substrate stabilize the enzyme |
664911 |
| 3.1.26.4 | partially purified enzyme extract is labile against freezing and dilution, addition of 45% glycerol |
655447 |
| 3.1.26.4 | ribonuclease H2 from Thermococcus kodakarensis is stabilized by its remarkably slow unfolding rate in guanidine hydrochloride, making the native state of RNase H2 completely resistant to subtilisin |
729225 |
| 3.1.26.4 | the C-terminal extension of the enzyme functions as a substrate-binding domain and stabilizes the RNase H domain |
729712 |
| 3.1.26.4 | the N-terminal extension of the enzyme functions as a substrate-binding domain and stabilizes the RNase H domain |
729712 |
