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It has been shown previously that the S-thiomethyl forms of the insulin A and B chains interact in solution leading to a partial transfer of Tyr side chains from hydrophilic to hydrophobic environments. In the present work, a circular dichroic study has indicated that the α-helix contents of the chains show a gradual increase upon mixing of the chains reaching completion in about 2h. The separated S-thiomethyl protected chains contain some ordered structure (A: α=15%, β=27%: B: α=22%, β=23%). Contrary to reports in the literature, the reduced chains also show some ordered structure and upon mixing of the reduced chains, the α-helix content also shows some increase. The ordered structure of the reduced chains decrease with increasing concentrations of dithiothreitel and in presence of a large excess of DTT both the reduced chains have very little, if any, α-helix structure. These latter results are in accord with those of Wu and Yang. In agreement with the results obtained previously with ultravio 相似文献
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