Two new structured intermediates in the oxidative folding of RNase A

FEBS Letters

Welker, Ervin¹  Volles, Michael J¹  Narayan, Mahesh¹  Scheraga, Harold A¹ 

[1] Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, NY 14853-1301, USA

关键词: Ribonuclease A;    Folding;    Dithiothreitol;    Oxidative refolding;    Disulfide bond;    Intermediate;    BPTI;    bovine pancreatic trypsin inhibitor;    RNase A;    bovine pancreatic ribonuclease A;    des-[40-95];    des-[65-72];    des-[26-84];    des-[58-110];    disulfide species of RNase A containing three native disulfide bonds but lacking the disulfide bond in brackets;    DTTox;    oxidized dithiothreitol;    DTTred;    D;    L-dithiothreitol (reduced dithiothreitol);    AEMTS;    2-aminoethylmethanethiosulfonate;    HPLC;    high performance liquid chromatography;    nS;    the ensemble of disulfide species with n disulfide bonds;   

DOI  :  10.1016/S0014-5793(99)01391-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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°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.

【 授权许可】

Unknown