Developments in small-angle X-ray scattering (SAXS) for characterizing the structure of surfactant-macromolecule interactions and their complex

Effect of heat treatment on the structural and emulsifying properties of copra meal protein: Improving interfacial properties to enhance performance of its Pickering emulsion

“…SAXS is a widely used technique for studying the submicroscopic structure of systems ( Chen et al, 2023 ). As shown in the Fig.…”

Evolution of the structure and interaction in the surfactant-dependent heat-induced gelation of protein

“…On addition of DTAB, the correlation peak disappears and the data show linearity in the intermediate Q range with two Q -cut offs, a clear signature of the protein unfolding and formation of beads-on-string kind of structure. 5,24,55 In this structure, the micelle-like beads are formed around the hydrophobic patches of the unfolded protein string. 5,47,56 The data are analyzed by combining the scattering contributions from protein–surfactant complexes (beads-on-string structure) and free micelles (if any).…”

“…The scattering from the beads-on-string structure is accounted for by a P ( Q ) of prolate ellipsoidal shape and S ( Q ) of random flight model, taking care of the structure and arrangement of DTAB micelles formed along the unfolded polypeptide chain, respectively. 46–48,55 The model fitting provides the size and number of micelles adsorbed per protein, as well as the distance between these micellar beads (Table 1). 47,48 The size of the micellar beads increases as the DTAB concentration increases, suggesting the enhanced protein unfolding.…”