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• W2039225949 endingPage "104" @default.
• W2039225949 startingPage "89" @default.
• W2039225949 abstract "The conformational study on cyclic Ac–Cys–Pro–Xaa–Cys–NHMe (Ac–CPXC–NHMe; X=Ala, Val, Leu, Aib, Gly, His, Phe, Tyr, Asn and Ser) peptides has been carried out using the Empirical Conformational Energy Program for Peptides, version 3 (ECEPP/3) force field and the hydration shell model in the unhydrated and hydrated states. This work has been undertaken to investigate structural implications of the CPXC sequence as the chain reversal for the initiation of protein folding and as the motif for active site of disulfide oxidoreductases. The backbone conformation DAAA is commonly the most feasible for cyclic CPXC peptides in the hydrated state, which has a type I β-turn at the Pro–Xaa sequence. The proline residue and the hydrogen bond between backbones of two cystines as well as the formation of disulfide bond appear to play a role in stabilizing this preferred conformation of cyclic CPXC peptides. However, the distributions of backbone conformations and β-turns may indicate that the cyclic CPXC peptide seems to exist as an ensemble of β-turns and coiled conformations in aqueous solution. The intrinsic stability of the cyclic CPXC motif itself for the active conformation seems to play a role in determining electrochemical properties of disulfide oxidoreductases." @default.
• W2039225949 created "2016-06-24" @default.
• W2039225949 creator A5072223518 @default.
• W2039225949 creator A5080601893 @default.
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• W2039225949 date "2003-08-01" @default.
• W2039225949 modified "2023-10-17" @default.
• W2039225949 title "Preferred conformations of cyclic Ac–Cys–Pro–Xaa–Cys–NHMe peptides: a model for chain reversal and active site of disulfide oxidoreductase" @default.
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• W2039225949 doi "https://doi.org/10.1016/s0301-4622(03)00139-x" @default.
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