Literature summary for 5.3.1.1 extracted from

Shi, Y.; Liu, J.H.; Zhang, H.J.; Ding, Y.
Equilibrium unfolding mechanism of chicken muscle triose phosphate isomerase (2008), Protein Pept. Lett., 15, 365-370.

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Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
unfolding of triosephosphate isomerase in urea is highly cooperative, and no folding intermediate is detected. The thermodynamic parameters just reflect the unfolding of dissociated folded monomer to fully unfolded monomer transition. Unfolding follows an irreversible two-state step with a slow aggregation process. The two subunits of the active enzyme unfold independently	Gallus gallus

Source Tissue

Source Tissue	Comment	Organism	Textmining
muscle	breast muscle	Gallus gallus	-

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Release 2023.1 (January 2023)