Laser Raman studies on cobrotoxin

• Published in: Biochimica et biophysica acta Vol. 537; no. 2; pp. 284 - 292
• Main Authors: Hseu, T.H., Chang, H., Hwang, D.M., Yang, C.C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 20.12.1978
• Subjects: Animals; Cobra Neurotoxin Proteins; Disulfides; Elapid Venoms; Hydrogen-Ion Concentration; Oxidation-Reduction; Protein Conformation; Species Specificity; Spectrum Analysis, Raman
• ISSN: 0005-2795; 0006-3002; 1879-2952
• DOI: 10.1016/0005-2795(78)90511-1

Laser Raman spectra of cobrotoxin under various conditions have been obtained. Comparison of the spectra of native cobrotoxin in lyophilized form and in aqueous solution indicates that the secondary structures of cobrotoxin are not significantly affected by the removal of the aqueous solvent. On going from the native to the partially reduced and the completely reduced, carboxymethylated forms, characteristic peaks of the C-S-S-C and tyrosine ring in the region of 500–900 cm −1 showed definite changes in structure. The partially reduced form gave two peaks at 502 and 524 cm −1, suggesting difference in the conformation of the remaining disulfide bonds. As indicated by the present work, the conformation of the main chain of cobrotoxin in the native unperturbed state, in the partially reduced and in the completely reduced forms are the coexistence of β-pleated sheet with random-coil structure, predominantly random coil, and predominantly random coil with the existence of an α-helix type structure, respectively. The effect of pH on the conformation of cobrotoxin in solution appeared to give rise to the change of the local structure of two aromatic residues common to all snake neurotoxins.