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Saxs study of structure and conformational changes of crotamine

✍ Scribed by Beltran, J.R.; Mascarenhas, Y.P.; Craievich, A.F.; Laure, C.J.

Book ID
118518596
Publisher
Biophysical Society
Year
1985
Tongue
English
Weight
254 KB
Volume
47
Category
Article
ISSN
0006-3495

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SAXS study of the snake toxin Ξ±-crotamin
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✍ J. R. Beltran; Y. P. Mascarenhas; A. F. Craievich; C. J. Laure πŸ“‚ Article πŸ“… 1990 πŸ› Springer 🌐 English βš– 401 KB

alpha-crotamine is a small toxic protein (42 amino acid residues with three disulphide bridges) present in the venom of Crotallus durissus terrificus. Molecular parameters (Rg = 13.7 A, S = 3,000 A2, V = 9,200 A3 and Dmax = 40 A) were derived from SAXS curves obtained from a solution of this protein