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Literature summary for 3.1.31.1 extracted from

  • Maki, K.; Cheng, H.; Dolgikh, D.A.; Roder, H.
    Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods (2007), J. Mol. Biol., 368, 244-255.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.31.1

Cloned(Commentary)

Cloned (Comment) Organism
recombinant Trp insertion enzymes Staphylococcus aureus

Protein Variants

Protein Variants Comment Organism
P47G/P117G/H124L/W140H tryptophan-free mutant used for the insertion of a unique tryptophan at positions 15, 27, 61, 76, 91, 102, and 121, mutant enzymes used to study the enzyme folding kinetics, variants are destabilized but maintain the ability to refold in the native-like structure Staphylococcus aureus

Organism

Organism UniProt Comment Textmining
Staphylococcus aureus
-
 unfolded enzyme
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme 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
15 80 temperature range for studying the thermal unfolding transitions Staphylococcus aureus
48
-
 melting point of the Trp91 insertion mutant enzyme Staphylococcus aureus
48.3
-
 melting point of the Trp15 insertion mutant enzyme Staphylococcus aureus
53
-
 melting point of the Trp102 insertion mutant enzyme Staphylococcus aureus
53
-
 melting point of the Trp61 insertion mutant enzyme Staphylococcus aureus
54.5
-
 melting point of the Trp27 insertion mutant enzyme Staphylococcus aureus
56.6
-
 melting point of the Trp76 insertion mutant enzyme Staphylococcus aureus
57
-
 melting point of the Trp121 insertion mutant enzyme Staphylococcus aureus
66.3
-
 melting point of the wild type enzyme Staphylococcus aureus