Please use this identifier to cite or link to this item: 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
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