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Magn Reson Chem. 2006 Jul;44 Spec No:S41-50.

NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids.

Author information

1
Institute for Molecular Bioscience and Australian Research Council Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane QLD 4072, Australia.

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.

PMID:
16826542
DOI:
10.1002/mrc.1821
[Indexed for MEDLINE]

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