New insight into the solution structures of wheat gluten proteins from Raman optical activity

Ewan W. Blanch, Donald D. Kasarda, Lutz Hecht, Kurt Nielsen, Laurence D. Barron

    Research output: Contribution to journalArticlepeer-review

    Abstract

    Vibrational Raman optical activity (ROA) spectra of the wheat proteins α-gliadin (A-gliadin), ω-gliadin, and a 30 kDa peptide called T-A-1 from the high molecular weight glutenin subunit (HMW-GS) Dx5 were measured to obtain new information about their solution structures. The spectral data show that, under the conditions investigated, A-gliadin contains a considerable amount of hydrated α-helix, most of which probably lies within a relatively structured C-terminal domain. Smaller quantities of β-structure and poly(L-proline) II (PPII) helix were also identified. Addition of methanol was found to increase the α-helix content at the expense of some of the β and PPII structure, In comparison, ω-gliadin and the T-A-1 peptide were found to consist of large amounts of well-defined PPII structure with some turns but no α-helix. The results for the T-A-1 peptide are in agreement with a model in which HMW-GS are extended but not highly rigid. Application of a pattern recognition technique, based on principal component analysis (PCA), to the ROA spectra reinforces these conclusions.
    Original languageEnglish
    Pages (from-to)5665-5673
    Number of pages8
    JournalBiochemistry
    Volume42
    Issue number19
    DOIs
    Publication statusPublished - 20 May 2003

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