Abstract
The renaturation of bovine pancreatic ribonuclease A and hen egg white lysozyme from their reduced forms involves two statistical processes, pairing of half-cystine residues by oxidation and rearrangement of disulfide bonds by enzyme or thiol catalyzed sulfhydryl-disulfide interchange. The stability against sulfhydryl-disulfide interchange of the native or nativelike conformation thus attained, which could be a form containing three native disulfide bonds and one open disulfide bond, causes the system to accumulate the renatured enzyme. Thus, the native-like conformation is associated with the lowest free energy only in the late phase of folding.
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Taniuchi, H., Acharya, A.S., Andria, G., Parker, D.S. (1977). On the Mechanism of Renaturation of Proteins Containing Disulfide Bonds. In: Friedman, M. (eds) Protein Crosslinking. Advances in Experimental Medicine and Biology, vol 86A. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-3282-4_4
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DOI: https://doi.org/10.1007/978-1-4684-3282-4_4
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