Literature summary for 4.6.1.18 extracted from

Volynskaya, A.V.; Kasumov, E.A.; Goldanskii, V.I.
An evidence for the equilibrium unfolding intermediates of ribonuclease A by tritium labeling method (2006), Int. J. Biol. Macromol., 39, 256-264.

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
the ribonuclease A equilibrium unfolding in urea and guanidinium chloride solutions proceeds through a formation of intermediates whose compactness, retention of the larger part hydrophobic core, secondary structure, and native-like folding pattern correspond to the wet molten globule state. The urea intermediate is less compact than that in GuCl. The refolding of the protein denatured by GuCl results in the formation of the intermediate which enzyme activity is virtually the same as the activity of the native protein	Bos taurus

Renatured (Comment)

Organism

the ribonuclease A equilibrium unfolding in urea and guanidinium chloride solutions proceeds through a formation of intermediates whose compactness, retention of the larger part hydrophobic core, secondary structure, and native-like folding pattern correspond to the wet molten globule state. The urea intermediate is less compact than that in GuCl. The refolding of the protein denatured by GuCl results in the formation of the intermediate which enzyme activity is virtually the same as the activity of the native protein

Bos taurus

Source Tissue

Source Tissue	Comment	Organism	Textmining
pancreas	-	Bos taurus	-

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Release 2023.1 (January 2023)