Literature summary for 3.1.31.1 extracted from

Paliwal, A.; Asthagiri, D.; Bossev, D.P.; Paulaitis, M.E.
Pressure denaturation of staphylococcal nuclease studied by neutron small-angle scattering and molecular simulation (2004), Biophys. J., 87, 3479-3492.

General Stability

General Stability	Organism
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

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

Organism	UniProt	Comment	Textmining
Staphylococcus sp.	-	-	-

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Release 2023.1 (January 2023)