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Reoxidation and renaturation studies on the main toxin of Naja naja samarensis
Author(s) -
Gacond J.J.,
Bargetzi J.P.,
Juillerat M.A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81252-1
Subject(s) - naja , cysteine , chemistry , glutathione , toxin , native state , disulfide bond , biophysics , folding (dsp implementation) , population , biochemistry , stereochemistry , venom , biology , enzyme , demography , sociology , electrical engineering , engineering
The main toxin of Naja naja samarensis is a very small and rigid protein ( M , 6850, 8 cysteines). When fully reduced, it regains its native conformation by a mechanism involving a rapid cysteine oxidation and a slower, less temperature‐dependent disulfide exchange. In a native‐like form of the protein we observed a population whose cysteines were incompletely reoxidized. When intermediates with blocked cysteines were incubated with oxidized and reduced glutathione, the percentage of native‐like molecules increased. These findings suggest a multiple folding pathway.