NMR of conotoxins: structural features and an analysis of chemical shifts of post-translationally modified amino acids
Contribuinte(s) |
Dr J. Keeler |
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Data(s) |
01/01/2006
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Resumo |
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 H-1 and C-13 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. Copyright (C) 2006 John Wiley & Sons, Ltd. |
Identificador | |
Idioma(s) |
eng |
Publicador |
John Wiley & Sons Ltd |
Palavras-Chave | #Nmr #Conotoxins #Post-translational Modification #Chemical Shifts #Conus #Venom #Chemistry, Multidisciplinary #Chemistry, Physical #Spectroscopy #Protein Secondary Structure #Gamma-carboxyglutamic Acid #3-dimensional Solution Structure #Snail Conus-geographus #Muscle Sodium-channels #Conantokin-g #Acetylcholine-receptors #Omega-conotoxins #Alpha-conotoxins #Cystine Knot #C1 #250302 Biological and Medical Chemistry #780105 Biological sciences |
Tipo |
Journal Article |