Predicted secondary structure of snake venom toxins from their primary structures.
We have predicted the secondary structure of 38 snake venom toxins using the  method of Chou and Fasman. Our predictions indicate that beta-chain and random coil structures predominate in these proteins. The conformations of long neurotoxins, short neurotoxins and cytotoxins are less similar than previously believed. Cytotoxins contain 40--50% of beta-structure and they form a notably homogeneous group. Short neurotoxins contain less beta-structure (13--30%) and more random coil than cytotoxins, and they also form a more heterogeneous group in terms of secondary structure. The characteristics of long neurotoxins are intermediate to the above mentioned groups. Experimental evidence supporting these propositions is discussed.
D000595:Amino Acid Sequence; D003603:Cytotoxins; D008961:Models, Structural; D008968:Molecular Conformation; D009498:Neurotoxins; D012910:Snake Venoms
D003603:Cytotoxins; D009498:Neurotoxins; D012910:Snake Venoms