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. 1986 Feb 1;233(3):731–736. doi: 10.1042/bj2330731

Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism.

G J van Holst, S R Martin, A K Allen, D Ashford, N N Desai, A Neuberger
PMCID: PMC1153092  PMID: 3707521

Abstract

The structure of potato (Solanum tuberosum) lectin, which is a hydroxyproline-rich glycoprotein, has been investigated by circular dichroism. The spectra of the native lectin, and of the oxidized, reduced and carboxymethylated and deglycosylated derivatives were examined, as was a hydroxyproline-rich glycopeptide and its deglycosylated derivative. It is concluded that the lectin contains about 35% polyproline II conformation, 34% type II beta-turn and 31% irregular conformation. No indications were found for the presence of alpha-helix or beta-sheet conformations. The polyproline II conformation is heat-stable, but is markedly destabilized by deglycosylation. The type II beta-turn is destabilized by cleavage of disulphide bonds.

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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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