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Literature summary for 4.6.1.24 extracted from
- Tryptophan conformations associated with partial unfolding in ribonuclease T1 (2009), Biophys. J., 97, 1778-1786.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | two extended replica-exchange molecular dynamics simulations on RNase T1, each with different histidine protonation states, corresponding to pH 6 and pH8. At high pH, the appearance of partially unfolded states is evident. This pH-induced destabilization originates from increased global repulsion as well as reduced local favorable electrostatic interactions and reduced H-bonding strength of His27, His40, and His92. At high pH, alternative tryptophan rotamers appear and are linked to a distorted environment of the tryptophan, which also acts as a separate source of ground-state heterogeneity | Aspergillus oryzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | P00651 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ribonuclease T1 | - |
Aspergillus oryzae |
| RNase T1 | - |
Aspergillus oryzae |
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Release 2023.1 (January 2023)
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