Journal of Agricultural and Food Chemistry · 1999 · 30 citations · 15 references
Natural SciencesBiochemistryMaterials ScienceBiomaterialsProtein BiochemistryStructural BiologyAtomic Force MicroscopyCellular UltrastructureProtein CondensatesProtein StructureSurface MicroscopyGliadin ChemistryPhase AngleProtein BodiesProtein FilmsProtein-surface InteractionsSurface PropertiesSurface Properties Of ProteinsTapping Mode Atomic Force Microscopy
Pure and mixed films of alpha- and omega-gliadins were studied by tapping mode atomic force microscopy (AFM). The technique was sensitive to the chemistry of the surface properties of the films, allowing imaging of the mixed gliadin phases at different ratios. In addition to the study of the phases at the micrometer level, higher resolution images allowed visualization of the protein films at the molecular level. These studies may have relevance to the formation of phases in developing protein bodies in grain, where gliadins and glutenins are deposited together. It has been assumed that the protein bodies consist of a random network of proteins; these studies indicate that microphases could be present in protein bodies. The technique provides novel methods for studying mixed biopolymer systems.
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Disulphide Bonds in Wheat Gluten Proteins
Peter R. Shewry, Arthur S. Tatham · Journal of Cereal Science · 1997 · 534 citations