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


Autoria(s): Marx, U. C.; Daly, N. L.; Craik, D. J.
Contribuinte(s)

Dr J. Keeler

Data(s)

01/01/2006

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

http://espace.library.uq.edu.au/view/UQ:80423

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