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  • Title: Two new structured intermediates in the oxidative folding of RNase A.
    Author: Welker E, Narayan M, Volles MJ, Scheraga HA.
    Journal: FEBS Lett; 1999 Nov 05; 460(3):477-9. PubMed ID: 10556520.
    Abstract:
    Two new three-disulfide intermediates have been found to be populated in the oxidative folding pathway of bovine pancreatic ribonuclease A at a low temperature (15 degrees C). These intermediates, des-[26-84] and des-[58-110], possess all but one of the four native disulfide bonds and have a stable tertiary structure, similar to the two previously observed intermediates, des-[65-72] and des-[40-95]. While the latter two des species each lack one surface-exposed disulfide bond, the newly discovered intermediates each lack one buried disulfide bond. The possible involvement of these species in the rate-determining steps during the oxidative folding of RNase A is discussed and a specific role for such species during oxidative folding is suggested.
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