Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A
- Authors
- Shin, H.-C.; Narayan, M.; Song, M.-C.; Scheraga, H.A.
- Issue Date
- 2003
- Citation
- Biochemistry, v.42, no.39, pp.11514 - 11519
- Journal Title
- Biochemistry
- Volume
- 42
- Number
- 39
- Start Page
- 11514
- End Page
- 11519
- URI
- http://scholarworks.bwise.kr/ssu/handle/2018.sw.ssu/21072
- DOI
- 10.1021/bi030152h
- ISSN
- 0006-2960
- Abstract
- To assess the role of the [65-72] disulfide bond in the oxidative folding of RNase A, use has been made of [C65S, C72S], a three-disulfide-containing mutant of RNase A which regenerates from its two-disulfide precursor in an oxidation and conformational folding-coupled rate-determining step. The distribution of disulfide bonds in the one-disulfide-containing ensemble of this mutant has been characterized. In general, the disulfide-bond distribution in its 1S ensemble agrees relatively well with the corresponding distribution in wt-RNase A and with distributions based on calculations of loop entropy, except for the absence of the [65-72] disulfide bond. There is no bias (over the entropic influence) for the three native disulfide bonds, [26-84], [40-95], and [58-110]. Previous oxidative folding results for wt-RNase A indicated the predominance of the des [40-95] intermediate over des [65-72] after the rate-determining step in the regeneration process. Considering that there is no preferential distribution of disulfides in the 1S ensemble of [C65S, C72S], in contrast to the preferential population of the [65-72] disulfide bond in wt-RNase A, these results indicate a critical role for the [65-72] disulfide bond in the regeneration of wt-RNase A. Furthermore, analysis of the disulfide distribution of the 1S intermediates of [C65S, C72S] compared to that of wt-RNase A lends support for a physicochemical basis for the previously observed slow folding rate of this mutant, compared to its analogue (des [65-72]) of wt-RNase A.
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