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Literature summary extracted from
- Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol (2001), Acta Crystallogr. Sect. D, 57, 1506-1512.
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 3.4.21.4 | vapour-diffusion hanging-drop technique, crystal structures of trypsin in presence of varying concentrations of polydocanol. Polydocanol binds to the protein with its hydrophilic head. There are at least 11 binding sites for polydocanol in trypsin. The hydrophilic binding of polydocanol results in cross-linked pairs of trypsin molecules | Sus scrofa |
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.4.21.4 | enhancement of stability and aggregation of proteins in the presence of low concentrations of polydocanol | Sus scrofa |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.4 | Sus scrofa | - |
- |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.4 | BPT | - |
Sus scrofa |
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Release 2023.1 (January 2023)
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