Oxidative folding of proteins.
The oxidative folding of proteins is reviewed and illustrated with bovine pancreatic ribonuclease A (RNase A). The mutual effects of conformational folding and disulfide bond regeneration are emphasized, particularly the "locking in" of native disulfide bonds by stable tertiary structure in disulfide intermediates. Two types of structured metastable disulfide species are discerned, depending on the relative protection of their disulfide bonds and thiol groups. Four generic pathways for oxidative folding are identified and characterized.
Narayan
M
M
Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14853-1301, USA.
Welker
E
E
Wedemeyer
W J
WJ
Scheraga
H A
HA
D000818:Animals; D002417:Cattle; D004220:Disulfides / Q000737:chemistry; D010084:Oxidation-Reduction; D017510:Protein Folding; D012259:Ribonuclease, Pancreatic / Q000737:chemistry
D004220:Disulfides; D012259:Ribonuclease, Pancreatic