General Stability | Organism |
---|---|
The structure and thermal stability of the protein are analyzed under different conditions by Fourier transform infrared spectroscopy and Molecular Dynamics simulations. The effects of SDS, pH, and temperature on the protein structure are characterized. The data indicated that pD affects differently the thermostability of alpha-helices and beta-sheets, and that 0.5% or higher SDS concentration have a significant repercussion on the structure | Pyrococcus furiosus |
Organic Solvent | Comment | Organism |
---|---|---|
SDS | The secondary structure of the protein is not affected by 0.1 or 0.2% of SDS. In the presence of 0.5%, the intensity of the alpha-helix band decreases markedly while the intensity of the beta-sheet band is slightly affected. In the presence of 0.7% SDS the beta-sheet band intensity decreases further and in the presence of 4% SDS it results very low | Pyrococcus furiosus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus furiosus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus furiosus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | computational analysis reveals the different behavior of the two active sites | Pyrococcus furiosus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
PfPDO | - |
Pyrococcus furiosus |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
pH affects differently the thermostability of alpha-helices and beta-sheets | Pyrococcus furiosus |
20 | - |
the C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0 | Pyrococcus furiosus |
100 | - |
flexibility increases with the pH, with a high value at pH 7.0 | Pyrococcus furiosus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
- |
Pyrococcus furiosus |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
5.8 | - |
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 | Pyrococcus furiosus |
7 | - |
the residual amide II band intensity is higher at pH 5.8 than at pH 7.0 suggesting that the acidic pH induces a more compact structure. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0 | Pyrococcus furiosus |
10 | - |
at pH 10.0 the protein undergoes partial unfolding. Decrease in alpha-helix content at pH 10.0, whereas the beta-sheet content remains unaltered. At pH 5.8, pH not optimum for the activity, and at 10°C and 100°C, the alpha2 helix region, where the N-terminal active site is localized, is less flexible than at pH 7.0 and pH 10.0. The C terminal active site at 20°C shows a reduced flexibility at all pH values, while at 100°C the flexibility increases with the pH, with a high value at pH 7.0 | Pyrococcus furiosus |