Conformational prediction for snake venom toxins and laser Raman scattering of a cardiotoxin from Taiwan cobra (Naja naja atra) venom
- 1 June 1977
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 16 (13) , 2999-3006
- https://doi.org/10.1021/bi00632a030
Abstract
Secondary structure regions in snake venom toxins were predicted using the prediction method of Chou and Fasman and an averaging scheme assuming structural homology in each type of toxins. In general, snake toxins contain only some .beta.-sheet regions and .beta. bends. The content of secondary structures thus predicted does vary to some extent. The predicted results correlate well with conclusions from physicochemical studies. Interestingly, .beta.-bend regions predicted for the 2 types of neurotoxins, short-neurotoxin-type and long-neurotoxin-type, are primarily located in the middle of disulfide loops in spite of large differences in primary sequences. Comparisons between predicted results and the crystal structure of erabutoxin b determined at 2.75 .ANG. resolution suggest that the 2 types of neurotoxin are both sequencely and conformationally related while cardiotoxins could have an entirely different molecular topology. The Raman spectrum of a Taiwan cobra cardiotoxin indicates that the content of .beta.-pleated-sheet structure could be greater than that in neurotoxins.This publication has 4 references indexed in Scilit:
- Three dimensional structure of erabutoxin b neurotoxic protein: inhibitor of acetylcholine receptor.Proceedings of the National Academy of Sciences, 1976
- Comparison of predicted and experimentally determined secondary structure of adenyl kinaseNature, 1974
- Circular Dichroism of Bence-Jones Proteins and Immunoglobulins G*The Journal of Biochemistry, 1968
- The disulfide bonds of cobrotoxin and their relationship to lethalityBiochimica et Biophysica Acta (BBA) - Protein Structure, 1967