title: Predicted secondary structure of snake venom toxins from their primary structures.
abstract: 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.
mesh_terms: D000595:Amino Acid Sequence; D003603:Cytotoxins; D008961:Models, Structural; D008968:Molecular Conformation; D009498:Neurotoxins; D012910:Snake Venoms
chemical_list: D003603:Cytotoxins; D009498:Neurotoxins; D012910:Snake Venoms