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Intrinsically disordered proteins (IDPs) show structural changes stimulated by changes in external conditions. This study aims to reveal the temperature dependence of the structure and dynamics of the intrinsically disordered region of Hef, one of the typical IDPs, using an integrative approach. Small-angle X-ray scattering (SAXS) and circular dichroism (CD) studies revealed that the radius of gyration and ellipticity at 222 nm remained constant up to 313-323 K, followed by a decline above this temperature range.

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Limited and unclear research exists on the individual capacity of major fractions of pea protein legumin (PL), vicilin (PV) and albumin (PA), which collectively contribute to the structural and functional properties of pea protein. Findings revealed that PV (72.26 ± 2.

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