Proceedings of the Korean Biophysical Society Conference (한국생물물리학회:학술대회논문집)
- 2001.06a
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- Pages.35-35
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- 2001
Preferred Conformations of Cyclic Ac-Cys-Pro-Xaa-Cys-NHMe Peptides： a Model for Chain Reversal and Active Site of Disulfide Oxidoreductase
- Park, Hae-Sook (Department of Radiotechnology, Cheju-halla College) ;
- Kim, Choonmi (College of Pharmacy, Ewha Womans University) ;
- Kang, Young-Kee (Department of Chemistry, Chungbuk National University)
- Published : 2001.06.01
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 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.(omitted)
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