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Literature summary for 3.6.4.10 extracted from
- Effect of the polypeptide binding on the thermodynamic stability of the substrate binding domain of the DnaK chaperone (2005), Biochim. Biophys. Acta, 1748, 1-8.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DnaK chaperone | - |
Escherichia coli |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
while the thermal unfolding of the beta-domain of DnaK384-638 is composed of two transitions in the presence of GdnHCl, the beta-domain of the substrate bound DnaK384-638 exhibits a single symmetrical DSC peak in the same condition | Escherichia coli |
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