Laser Raman spectroscopy of snake venom neurotoxins: conformation.
Laser Raman spectra of neurotoxins of Pelamis platurus (yellow-bellied sea snake) and Laticauda semifasciata (broad-banded blue sea snake) were investigated. The amide I band appeared at 1672 cm-1 for both toxins, which presents an indication of anti-parallel beta structure. Since this agrees well with the result from the CD-ORD studies of snake neurotoxin, it was concluded that snake neurotoxins mainly consist of beta structure. The amide III band appeared at 1245 cm-1 for P. platurus toxin and 1248 cm-1 for L. semifasciata toxin. The four disulfide bonds present in the toxin have a very similar geometry. After vigorous heat treatment, the backbone configuration of the toxin molecule basically remained the same although it was partially denatured. The major peak at 512 cm-1 was not altered by the heat treatment but a new shoulder appeared at 546 cm-1. This suggests that a new type of S-S stretching vibration (trans-gauche-trans) was produced as a result of heat treatment. However, the majority of the S-S vibrations remained in the gauche-gauche-gauche orientation. A substantial change in the interactions between a tyrosine aromatic ring and neighboring residues was apparently the alteration caused by the heat treatment.
D000596:Amino Acids / Q000032:analysis; D002942:Circular Dichroism; D006358:Hot Temperature; D007834:Lasers; D011485:Protein Binding; D011487:Protein Conformation; D012910:Snake Venoms / Q000032:analysis*; D013057:Spectrum Analysis; D014118:Toxins, Biological / Q000032:analysis*
D000596:Amino Acids; D012910:Snake Venoms; D014118:Toxins, Biological