Literature summary for 5.3.1.1 extracted from

Moreau, V.H.; Rietveld, A.W.; Ferreira, S.T.
Persistent conformational heterogeneity of triosephosphate isomerase: separation and characterization of conformational isomers in solution (2003), Biochemistry, 42, 14831-14837.

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Organic Solvent Stability

Organic Solvent	Comment	Organism
guanidine-HCl	dissociation/unfolding is a highly cooperative transition in which the ternary and the secondary structures of the protein are concomitantly lost. Isolation of two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	-	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
two conformational isomers of the enzyme that exhibit significantly different stabilities and kinetics of unfolding. Complete unfolding of the two isolated conformers at a 1.5 M guanidine-HCl followed by refolding by removal of the denaturant completely abolishes the differences in their unfolding kinetics	Oryctolagus cuniculus

Source Tissue

Source Tissue	Comment	Organism	Textmining

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Release 2023.1 (January 2023)