In:
Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 68, No. 9 ( 1971-09), p. 2173-2176
Abstract:
The pH dependence of the conformation of concanavalin A has been studied by means of optical rotatory dispersion and circular dichroism spectroscopy. At pH 2.9, 5.0, and 7.0, the major contribution to organized structure appears to be the β conformation. At pH 9.1, the conformation of concanavalin A approaches the random coil or unordered form. No evidence could be found for the presence of any significant amount of α helix. The pH of maximum precipitin-like activity of concanavalin A is paralleled by the pH dependence of the parameter b 0 in the Moffitt equation.
Type of Medium:
Online Resource
ISSN:
0027-8424
,
1091-6490
DOI:
10.1073/pnas.68.9.2173
Language:
English
Publisher:
Proceedings of the National Academy of Sciences
Publication Date:
1971
detail.hit.zdb_id:
209104-5
detail.hit.zdb_id:
1461794-8
SSG:
11
SSG:
12
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