SAXS study of crotapotin at low pH
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Data
1993-02-01
Autores
Abrego, José Ramon Beltran [UNESP]
Craievich, Aldo Felix
Mascarenhas, Yvonne Primerano
Laure, Carlos J.
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Biophysical Society
Resumo
The structure of crotapotin, a protein extracted from the venom of the Crotalus durissus terrificus, in solution at pH = 1.5, was studied by SAXS. The experimental results yield structural parameter values of the molecular radius of gyration R(g) = 13.6 angstrom, volume v = 16.2 x 10(3) angstrom3 and maximal dimension D(max) = 46 angstrom. The distance distribution function deduced from the scattering measurements is consistent with an overall molecular shape of an oblate ellipsoid of revolution with assymetry parameter nu = 0.45.
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Biophysical Journal. Bethesda: Biophysical Society, v. 64, n. 2, p. 560-564, 1993.