NMR studies of a neurotoxin (candoxin) from Bungarus candidus -presence of a predominantly β-sheet structure

Abstract

Complete sequence-specific 1H resonance assignments of a neurotoxin, candoxin, from Bungarus candidus has been reported. Qualitative interpretation of the nOes, chemical shift indices and deuterium exchange rates indicate a highly ordered and rigid conformation for this protein with an extended conformation for more than 50% of the residues and the complete absence of α-helical segments.