PREDICTED SECONDARY STRUCTURE OF SNAKE VENOM TOXINS FROM THEIR PRIMARY STRUCTURES

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Abstract
The secondary structure of 38 snake venom toxins using the method of Chou and Fasman were predicted. The 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% .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.

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