Small-angle neutron scattering studies from solutions of bovine nasal cartilage proteoglycan [electronic resource].
- Hoboken, N.J. : Stevens Institute of Technology, 1985. and Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Physical Description:
- Pages: 12 : digital, PDF file
- Additional Creators:
- Stevens Institute of Technology and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- Small-angle neutron scattering, SANS, of the proteoglycan subunit of bovine nasal cartilage in 0.15N LiCl at 25/sup 0/C yielded the radius of gyration, R/sub g/, radius of gyration of the cross-section, R/sub q/, persistence length, a, and the molecular weight, M. The following values were obtained: M = 3.9 x 10/sup 6/, R/sub g/ = 745 A, R/sub q/ = 34.6 A and a = 35.2 A. These values compare favorably with those that were obtained from small angle x-ray scattering, SAXS, of a similar extract. The scattering curve of the proteoglycan subunit in D/sub 2/O showed a characteristic broad peak in the specified angular range similar to that observed from SAXS, thus confirming the polyelectrolyte nature of the proteoglycan. 15 refs., 3 figs., 1 tab. (DT)
- Published through SciTech Connect., 08/01/1985., "conf-850871-7", "DE85016935", International conference on neutron scattering, Santa Fe, NM, USA, 19 Aug 1985., and Patel, A.; Gregory, J.D.; Bunick, G.J.; Uberbacher, E.C.; Stivala, S.S.; Damle, S.P.
- Funding Information:
View MARC record | catkey: 13814037