Conformational Analysis of Snake Toxins by Laser Raman Spectroscopy
Conformations of snake toxins, neurotoxins and hemorrhagic toxin were analyzed by laser Raman spectroscopy. All sea snake neurotoxins consist of antiparallel β-sheet and β-reverse turn structures. Hemorrhagic toxin e isolated from western diamondback rattlesnake is a zinc dependent protease. Judging from the Raman spectra, hemorrhagic toxin e consists of some α-helix with a high degree of random coil or β-reverse turn structure. All these toxins have gauche-gauche-gauche conformation of C-C-S-S-C-C according to S-S stretching vibration frequency. The tyrosine residue of most sea snake neurotoxins is buried as I830 is stronger than I850. From the 1361 cm−1 band, it is concluded that the tryptopnan residue of neurotoxins is exposed to the outside of the molecule.
KeywordsZinc Benzene Tyrosine Amide Cysteine
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