General Stability | Organism |
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pressure denaturation of staphylococcal nuclease over a pressure range of 1-3 kilobars at 25°C is studied by neutron small-angle scattering and molecular simulation. The globular structure of the enzyme is retained across the folding/unfolding transition although this structure is less compact and elongated relative to the native structure. The findings support a mechanism for the pressure-induced unfolding of the enzyme in which water penetration into the hydrophobic core plays a central role | Staphylococcus sp. |
Organism | UniProt | Comment | Textmining |
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Staphylococcus sp. | - |
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