This work is supported by the Biomedical Research Council, Agency for Science, Technology, and Research, Singapore. T.S.K. acknowledges the Singapore Millennium Foundation for granting the research scholarship. The authors thank the Sophisticated Instrument Facility at the Indian Institute of Science and the Chemical and Molecular Analysis Center, Department of Chemistry at the National University of Singapore for allowing the use of their NMR spectrometers.
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Communication
Effect of C-Terminal Amidation on Folding and Disulfide-Pairing of α-Conotoxin ImI†
Article first published online: 14 SEP 2005
DOI: 10.1002/anie.200502300
Copyright © 2005 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
Additional Information
How to Cite
Kang, T. S., Vivekanandan, S., Jois, S. D. S. and Kini, R. M. (2005), Effect of C-Terminal Amidation on Folding and Disulfide-Pairing of α-Conotoxin ImI. Angew. Chem. Int. Ed., 44: 6333–6337. doi: 10.1002/anie.200502300
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Publication History
- Issue published online: 30 SEP 2005
- Article first published online: 14 SEP 2005
- Manuscript Revised: 26 JUL 2005
- Manuscript Received: 1 JUL 2005
Keywords:
- amidation;
- neurotoxins;
- NMR spectroscopy;
- peptides;
- protein folding
Building bridges: α-Conotoxins (C1–C3, C2–C4 disulfide pairing) adopt a globular conformation, whereas χ/λ-conotoxins (C1–C4, C2–C3 disulfide pairing) fold into a ribbon conformation. Amidation of the peptide C terminus has been shown to influence the folding (see picture) and hence the biological activity of conotoxins.