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- W2023295637 abstract "Wheat germ agglutinin (WGA), a lectin binding a N ‐acetyl‐ D ‐neuraminic acid (NeuNAc) and/or N ‐acetyl‐ D ‐glucosamine (GlcNAc) group, was studied by Fourier transform infrared (FTIR) spectroscopy. Deconvolution of the FTIR spectrum of WGA alone indicated the presence of few α‐helices and β‐sheets, in contrast to many other lectins. These results agree with previous WGA crystal data. The WGA conformational changes, induced by GlcNAc‐bearing liposomes or GlcNAc oligomers, were studied by infrared differential spectroscopy. The GlcNAc binding to WGA resulted in a decrease of turns and α‐helices and a concomitant appearance of β‐sheets, inducing more or less peptidic N‐H deuteration." @default.
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- W2023295637 date "1999-08-11" @default.
- W2023295637 modified "2023-10-17" @default.
- W2023295637 title "A FTIR spectroscopy evidence of the interactions between wheat germ agglutinin and<i>N</i>-acetylglucosamine residues" @default.
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- W2023295637 doi "https://doi.org/10.1016/s0014-5793(99)00981-3" @default.
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