Premium
Effect of C‐Terminal Amidation on Folding and Disulfide‐Pairing of α‐Conotoxin ImI
Author(s) -
Kang Tse Siang,
Vivekanandan Subramanian,
Jois Seetharama D. S.,
Kini R. Manjunatha
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200502300
Subject(s) - pairing , disulfide bond , conotoxin , folding (dsp implementation) , chemistry , protein folding , ribbon , peptide , stereochemistry , biochemistry , physics , mathematics , geometry , engineering , superconductivity , quantum mechanics , electrical engineering
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.