We report C-13 NMR assignments of a weak neurotoxin called candoxin, using
heteronuclear single quantum correlation (HSQC) experiments with their natu
ral abundance in the protein. Almost complete sequence-specific C-13 NMR as
signments were achieved. Chemical shift indices of C-13(alpha), C-13(beta)
and H-1(alpha) were used to characterize the secondary structural segments
in the protein. A consensus plot of chemical shift indices revealed five be
ta -strands as the major structural elements in the toxin. Copyright (C) 20
01 John Wiley & Sons, Ltd.