PMID: 591177Oct 1, 1977

Conformational stability of a snake cardiotoxin

International Journal of Peptide and Protein Research
M C Hung, Y H Chen


A snake cardiotoxin from the venom of the Formosan cobra, Naja naja atra, is a basic polypeptide. The protein can be denatured in 6.0 M guanidine hydrochloride or at elevated temperatures. Its conformation remains virtually the same in solvents of lower polarity than water such as 1, 2-ethanediol or 1-propanol and 1, 2-ethanediol (1:1 v/v). The circular dichroism spectrum is atypical in water in that the peptide chromophores show a small negative CD band at 214 nm and a large positive one at 195 nm. To some extent the CD pattern resembles that of the beta-form but differs in specific positions and magnitudes. Considering that the theoretical CD of the reverse beta-bend and the characteristics of model polypeptides in beta-form manifest a similar pattern, we suggest that cobra cardiotoxin is rich in beta structure including beta pleated-sheets and beta reverse-turns.


May 3, 1977·Biochemistry·Y H ChenJ T Yang
Jan 1, 1968·Naunyn-Schmiedebergs Archiv für experimentelle Pathologie und Pharmakologie·C Y LeeS Y Lee
Jan 15, 1974·Biochemistry·P Y Chou, G D Fasman
Oct 23, 1970·Biochemical and Biophysical Research Communications·K Narita, C Y Lee
Oct 21, 1968·Biochimica Et Biophysica Acta·C C YangK Hamaguchi


Jan 1, 1983·CRC Critical Reviews in Biochemistry·M J Dufton, R C Hider
Jan 24, 1998·Journal of Biomolecular Structure & Dynamics·T K KumarC Yu
Mar 1, 1978·International Journal of Peptide and Protein Research·K NaritaT B Lo
Apr 1, 1980·European Journal of Biochemistry·A DrakeR C Hider
Jan 1, 1987·Journal of Molecular Evolution·R Breckenridge, M J Dufton

Related Concepts

Circular Dichroism, Vibrational
Cobra Venoms
Protein Conformation
Spectrophotometry, Ultraviolet

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