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.
Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism
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G J van Holst, S R Martin, A K Allen, D Ashford, N N Desai, A Neuberger; Protein conformation of potato (Solanum tuberosum) lectin determined by circular dichroism. Biochem J 1 February 1986; 233 (3): 731–736. doi: https://doi.org/10.1042/bj2330731
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