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. 1971 Sep;68(9):2173–2176. doi: 10.1073/pnas.68.9.2173

pH-Dependent Conformational Changes of Concanavalin A

R Zand 1,2, B B L Agrawal 1,2,*, I J Goldstein 1,2
PMCID: PMC389378  PMID: 5289376

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 b0 in the Moffitt equation.

Keywords: Moffitt equation, ORD spectra, CD spectra, precipitin, protein structure

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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