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Literature summary for 1.8.1.8 extracted from
- High hydrostatic pressure-induced conformational changes in protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus. A fourier-transform infrared spectroscopic study (2010), Mol. Biosyst., 6, 2015-2022 .
General Stability
| General Stability | Organism |
|---|---|
| the enzyme is highly piezostable. The effect of pressure on the molecule is not uniform and that different areas of the protein can have different local compressibility and resistance to high hydrostatic pressure. alpha-Helices are more sensitive than beta-sheets to pressure up to 5 kbar, whilst within 5.1-8.0 kbar the loss of eta-sheets is more pronounced than the loss of alpha-helices | Pyrococcus furiosus |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pyrococcus furiosus | - |
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Release 2023.1 (January 2023)
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