EC Number   |
Temperature Stability Minimum [°C] |
Temperature Stability Maximum [°C] |
Reference |
|---|
   3.1.26.4 | -999 |
- |
analysis of thermal unfolding, the folding core of Chlorobium tepidum RNaseH plays an important role in the unfolded state of this protein |
714194 |
| 3.1.26.4 | -999 |
- |
analysis of thermal unfolding, the folding core of Thermus thermophilus RNaseH plays an important role in the unfolded state of this protein |
714194 |
| 3.1.26.4 | -999 |
- |
comparison of thermostability of wild-type and mutant enzymes, overview |
715581 |
| 3.1.26.4 | -999 |
- |
melting temperature is 66°C, conserved quantitative stability/flexibility relationships, QSFR, thermodynamics, thermal stability and flexibility of the enzyme |
666879 |
| 3.1.26.4 | -999 |
- |
melting temperature is 86°C, conserved quantitative stability/flexibility relationships, QSFR, thermodynamics, thermal stability and flexibility of the enzyme |
666879 |
| 3.1.26.4 | -999 |
- |
melting temperatures for duplexes of antisense oligodeoxynucleotide with RNA-15 and RNA-20 were 63°C and 70°C, respectively |
677553 |
| 3.1.26.4 | -999 |
- |
stabilization of the thermostable enzyme is enhanced with increased salt concentration (Mg2+ or K+) |
726556 |
| 3.1.26.4 | -999 |
- |
structures and mechanism of thermostability |
657146 |
| 3.1.26.4 | -999 |
- |
the C-terminal of RNase HI from the hyperthermophile Sulfolobus tokodaii does not affect overall structure, and thermal stabilization is caused by local interactions of the C-terminal, suggesting that the C-terminal residues could be used as a stabilization tag. Thermodynamic measurements of the stability of variants lacking the disulfide bond, C58/145A, or the six C-terminal residues (DELTAC6) and by structural analysis of DELTAC6, overview |
716693 |
| 3.1.26.4 | -999 |
- |
the C-terminus tail (G144-T149) of the RNase HI plays an important role in hyperstabilization of this protein |
725763 |
