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  • Title: Circular dichroism and conformational transition of Dolichos biflorus and Robinia pseudoacacia lectins.
    Author: Père M, Bourrillon R, Jirgensons B.
    Journal: Biochim Biophys Acta; 1975 May 30; 393(1):31-6. PubMed ID: 1138924.
    Abstract:
    The conformation of the lectins from Dolichos biflorus and Robinia pseudoacacia was studied by means of circular dichroism (CD). It was found that N-acetyl-D-galactosamine induced significant changes in the near-ultraviolet CD spectrum of Dolichos lectin but was ineffective with the lectin from Robinia. Tyrosine and tryptophan chromophores were chiefly involved in this saccharide-lectin interaction. The far-ultraviolet CD spectra indicated that both lectins have a significant content of the pleated sheet conformation, but not much, if any, alpha-helix. The predominant conformation in these lectins is the aperiodic bend structure which is stabilized chiefly by hydrophobic interactions. This was ascertained by the effect of sodium dodecylsulfate on these proteins.
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