This work was supported by the National Creative Research Initiative Program of the Ministry of Education, Science and Technology.
Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide†
Article first published online: 22 JAN 2009
Copyright © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Angewandte Chemie International Edition
Volume 48, Issue 9, pages 1601–1605, February 16, 2009
How to Cite
Lim, Y.-b., Moon, K.-S. and Lee, M. (2009), Stabilization of an α Helix by β-Sheet-Mediated Self-Assembly of a Macrocyclic Peptide. Angew. Chem. Int. Ed., 48: 1601–1605. doi: 10.1002/anie.200804665
- Issue published online: 10 FEB 2009
- Article first published online: 22 JAN 2009
- Manuscript Revised: 12 DEC 2008
- Manuscript Received: 23 SEP 2008
- Ministry of Education, Science and Technology
- helical structures;
- protein models;
Protein roll call: Peptide-based building blocks, in which both an α-helix-forming segment and a β-sheet segment are located within a single macrocyclic structure, self-assemble into α-helix-decorated artificial proteins. This approach provides a starting point for developing artificial proteins that can modulate α-helix-mediated interactions occurring in a multivalent fashion.