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Literature summary for 3.1.31.1 extracted from

  • Kato, S.; Kamikubo, H.; Hirano, S.; Yamazaki, Y.; Kataoka, M.
    Nonlocal interactions are responsible for tertiary structure formation in staphylococcal nuclease (2010), Biophys. J., 98, 678-686.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
wild type and mutant Snases are expressed in Escherichia coli BL-21 (DE3) as inclusion bodies Staphylococcus sp.

Protein Variants

Protein Variants Comment Organism
Y54C/I139C production by site-directed mutagenesis, the oxidized form assumes a more compact denatured structure under acidic conditions than the wild type, the kinetic measurements reveal that the refolding reactions of both the reduced and oxidized forms of mutant are similar to those of the wild type protein Staphylococcus sp.
Y54C/I139C/DELTA140-149 production by site-directed mutagenesis, under physiological conditions, the reduced form appears to assume a denatured structure, in contrast, the oxidized form forms a native-like structure Staphylococcus sp.

Organism

Organism UniProt Comment Textmining
Staphylococcus sp.
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-
-

Purification (Commentary)

Purification (Comment) Organism
wild type and mutant enzyme are purified by a series of urea extraction, ethanol precipitation, and ion exchange chromatography Staphylococcus sp.

Synonyms

Synonyms Comment Organism
SNase
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Staphylococcus sp.
staphylococcal nuclease
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Staphylococcus sp.