title: NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids.
abstract: Conotoxins are small conformationally constrained peptides found in the venom of marine snails of the genus Conus. They are usually cysteine rich and frequently contain a high degree of post-translational modifications such as C-terminal amidation, hydroxylation, carboxylation, bromination, epimerisation and glycosylation. Here we review the role of NMR in determining the three-dimensional structures of conotoxins and also provide a compilation and analysis of 1H and 13C chemical shifts of post-translationally modified amino acids and compare them with data from common amino acids. This analysis provides a reference source for chemical shifts of post-translationally modified amino acids.
authors.affiliation: Institute for Molecular Bioscience and Australian Research Council Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane QLD 4072, Australia.
authors.forename: Ute C
authors.initials: UC
authors.lastname: Marx
authors.forename: Norelle L
authors.initials: NL
authors.lastname: Daly
authors.forename: David J
authors.initials: DJ
authors.lastname: Craik
mesh_terms: D000596:Amino Acids / Q000032:analysis*; D000818:Animals; D002247:Carbon Isotopes / Q000032:analysis; D020916:Conotoxins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D011522:Protons
chemical_list: D000596:Amino Acids; D002247:Carbon Isotopes; D020916:Conotoxins; D011522:Protons