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Preferred conformations of cyclic Ac-Cys-Pro-Xaa-Cys-NHMe peptides: A model for chain reversal and active site of disulfide oxidoreductase

Title
Preferred conformations of cyclic Ac-Cys-Pro-Xaa-Cys-NHMe peptides: A model for chain reversal and active site of disulfide oxidoreductase
Authors
Park H.S.Kim C.Kang Y.K.
Ewha Authors
김춘미
SCOPUS Author ID
김춘미scopus
Issue Date
2003
Journal Title
Biophysical Chemistry
ISSN
0301-4622JCR Link
Citation
vol. 105, no. 1, pp. 89 - 104
Indexed
SCI; SCIE; SCOPUS WOS scopus
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. © 2003 Elsevier B.V. All rights reserved.
DOI
10.1016/S0301-4622(03)00139-X
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약학대학 > 약학과 > Journal papers
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