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https://doi.org/10.1002/anie.200502300
| Title: | Effect of C-terminal amidation on folding and disulfide-pairing of α-conotoxin ImI | Authors: | Kang, T.S. Vivekanandan, S. Jois, S.D.S. Kini, R.M. |
Keywords: | Amidation Neurotoxins NMR spectroscopy Peptides Protein folding |
Issue Date: | 7-Oct-2005 | Citation: | Kang, T.S., Vivekanandan, S., Jois, S.D.S., Kini, R.M. (2005-10-07). Effect of C-terminal amidation on folding and disulfide-pairing of α-conotoxin ImI. Angewandte Chemie - International Edition 44 (39) : 6333-6337. ScholarBank@NUS Repository. https://doi.org/10.1002/anie.200502300 | Abstract: | (Figure Presented) 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. © 2005 Wiley-VCH Verlag GmbH & Co. KGaA. | Source Title: | Angewandte Chemie - International Edition | URI: | http://scholarbank.nus.edu.sg/handle/10635/52887 | ISSN: | 14337851 | DOI: | 10.1002/anie.200502300 |
| Appears in Collections: | Staff Publications |
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