Literature summary for 3.1.31.1 extracted from

Erlkamp, M.; Grobelny, S.; Winter, R.
Crowding effects on the temperature and pressure dependent structure, stability and folding kinetics of Staphylococcal nuclease (2014), Phys. Chem. Chem. Phys., 16, 5965-5976.

Search for more literature for 3.1.31.1

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
16800	-	-	Staphylococcus aureus

Organism

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	P00644	-	-

Subunits

Subunits	Comment	Organism
monomer	1 * 16800	Staphylococcus aureus
More	the enzyme contains 26.2% alpha-helices, 24.8% beta-sheets, 26.8% beta-turns, 8.7% unordered chains and 7.4% extended chains (6.1% is uncertain), PDB ID: 1STN	Staphylococcus aureus

Synonyms

Synonyms	Comment	Organism
SNase	-	Staphylococcus aureus
staphylococcal nuclease	-	Staphylococcus aureus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
additional information	-	temperature- and pressure-dependent stability diagram, thermodynamic properties, and folding reaction kinetics of the small, single-domain monomeric staphylococcal nuclease in presence or absence of macromolecular crowder agent Ficoll PM 70, which behaves as a semi-rigid spheroid with a hydrodynamic radius of about 5 nm, detailed overview. Increasing the temperature from 25°C to 57°C exhibits no change of the size of the crowder particles within the experimentalerror. No significant changes in particle size are detected by raising the pressure up to 2.5 kbar. The measured translational diffusion times indicate that, depending on the size of the protein, themicroviscosity of Ficoll PM70 is only about 4-6 times larger than the microviscosity of pure water	Staphylococcus aureus

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Release 2023.1 (January 2023)