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- W3089609840 abstract "The partial enzymatic hydrolysis of wheat gliadins constitutes an interesting tool to unravel their structural specificity. In this work, the structure and conformation of γ-gliadin were investigated through its limited chymotrypsic digestion. Using a combination of computational, biochemical and biophysical tools, we studied each of its N and C terminal domains. Our results reveal that γ-gliadin is a partially disordered protein with an unfolded N-terminal domain surprisingly resistant to chymotrypsin and a folded C-terminal domain. Using spectroscopic tools, we showed that structural transitions occured over the disordered N-terminal domain for decreasing ethanol/water ratios. Using SAXS measurements, low-resolution 3D structures of γ-gliadin were proposed. To relate the repeated motifs of the N-terminal domain of γ-gliadin to its structure, engineered peptide models PQQPY/F were also studied. Overall results demonstrated similarities between the N-terminal domain and its derived model peptides. Our findings support the use of these peptides as general templates for understanding the wheat protein assembly and dynamics." @default.
- W3089609840 created "2020-10-08" @default.
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- W3089609840 date "2020-12-01" @default.
- W3089609840 modified "2023-10-16" @default.
- W3089609840 title "New exploration of the γ-gliadin structure through its partial hydrolysis" @default.
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- W3089609840 doi "https://doi.org/10.1016/j.ijbiomac.2020.09.136" @default.
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