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Literature summary for 4.6.1.18 extracted from
- Correlation of folding kinetics with the number and isomerization states of prolines in three homologous proteins of the RNase family (2006), FEBS Lett., 580, 5029-5032.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
- |
- |
| Lithobates pipiens | - |
- |
- |
Renatured (Commentary)
| Renatured (Comment) | Organism |
|---|---|
| comparison of folding kinetics with bovine RNase A and angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases | Lithobates pipiens |
| comparison of folding kinetics with Rana pipiens' onconase and bovine angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases | Bos taurus |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| More | comparison of folding kinetics with bovine RNase A and angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases | Lithobates pipiens |
| More | comparison of folding kinetics with Rana pipiens' onconase and bovine angiogenin at pH 8.0 and 15°C. Direct correlation between the number of cis-prolyl bonds in a native protein and the complexity with which it folds via slower phases | Bos taurus |
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