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Small‐angle x‐ray scattering of bovine nasal cartilage proteoglycan in solution
Author(s) -
Stivala S. S.,
Patel A.,
Khorramian B.,
Gregory J. D.,
Damle S.
Publication year - 1987
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360260507
Subject(s) - small angle x ray scattering , chemistry , radius of gyration , scattering , gyration , radius , intrinsic viscosity , axial ratio , crystallography , prolate spheroid , molecular physics , analytical chemistry (journal) , polymer , chromatography , optics , geometry , physics , microstrip , mathematics , computer security , organic chemistry , classical mechanics , computer science , circular polarization
The proteoglycan subunit (PGS) from bovine nasal cartilage was examined in water and in 0.15 N LiCl by small‐angle x‐ray scattering (SAXS). The molecular weight of 2.5 × 10 6 and the radius of gyration, R g = 493 Å, in 0.15 N LiCl, obtained by SAXS, are in good agreement with values reported by others for similar preparations. Values of the radius of gyration of the cross section, mass per unit length, and persistence length of the PGS are also reported. The low value of intrinsic viscosity ([η]) found in 0.15 N LiCl, and a comparison of the experimental distance distribution function to that of the theoretical distance distribution function for sphere, suggest that the PGS in salt solution approaches spherical symmetry. The much higher value of [η] in water suggests a prolate ellipsoid of low axial ratio.