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General review on the oxidative folding of small disulfide-rich proteins are available [Arolas et al, 2006; Craik 2010]. |
Carboxypeptidase inhibitor |
The Knottin PCI folds in a complex processThe folding pathway of the Potato Carboxypeptidase A Inhibitor
PCI has been analyzed by structural analysis and stop/go folding
experiments [Chang
et al., 1994]. Comparison with other small disulfide-rich proteins show that proteins such as PCI with their native disulfide bonds reduced in a collective and simultaneous manner exhibit both a high degree of heterogeneity of folding intermediates and the accumulation of scrambled isomers along the folding pathway [Chang & Bulychev, 2000a]. Analysis of the unfolding pathway of PCI has revealed the existence of structurally defined unfolding intermediates [Chang et al., 2000b]. It was also shown that the PCI sequence is unable to fold quantitatively into a single native structure, and that, under physiological conditions, the scrambled isomers of PCI that constitute about 4% of the protein are in equilibrium with native PCI. PCI folding does not depend on the prosequenceFolding of the Potato Carboxypeptidase A Inhibitor PCI has
been studied with or without the prosequences, either in vitro
or in vivo in Escherichia coli [Bronsoms
et al., 2003]. |