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SYNOPSISThe mechanical properties of composites of granular starch and low density polyethylene (PE) have been studied as functions of starch volume fraction 4, granule size, and presence of compatibilizer. Property-volume fraction relationships were interpreted using various theories of composite properties. The dependence of elongation (t -41/3) and tensile strength ( IJ -@I3) agree with theoretical predictions, although the proportionality constants are less negative than theoretical values. The addition of compatibilizer (ethylene-co-acrylic acid copolymer, EAA) did not significantly affect the elongation or tensile strength, but significantly increased the composite tensile modulus. The cornstarch/PE moduli could be described by the Kerner or Halpin-Tsai equations. Analysis of the composite moduli data using the Halpin-Tsai equation allowed the estimation of the modulus of granular starch. The value obtained, 15 GPa, is considerably greater than most unfilled synthetic polymers of commercial importance, but significantly lower than the modulus of cellulose. It is also greater than a previously reported value of 2.7 GPa.

A variety of published physical measurements, computational algorithms, and structural modeling methods have been used to create a molecular model of 19 kDa alpha-zein (Z19). Zetaeins are water-insoluble storage proteins found in corn protein bodies. Analyses of the protein sequence using probability algorithms, structural studies by circular dichroism, infrared spectroscopy, small-angle X-ray scattering (SAXS), light scattering, proton exchange, NMR, and optical rotatory dispersion experiments suggest that Z19 has approximately 35-60% helical character, made up of nine helical segments of about 20 amino acids with glutamine-rich "turns" or "loops". SAXS and light-scattering experiments suggest that in alcohol/water mixtures alpha-zein exists as an oblong structure with an axial ratio of approximately 6:1. Furthermore, ultracentifugation, birefringence, dielectric, and viscosity studies indicate that alpha-zein behaves as an asymmetric particle with an axial ratio of from 7:1 to 28:1. Published models of alpha-zein to date have not been consistent with the experimental data, and for this reason the structure was re-examined using molecular mechanics and dynamics simulations creating a new three-dimensional (3D) structure for Z19. From the amino acid sequence and probability algorithms this analysis suggested that alpha-zein has coiled-coil tendencies resulting in alpha-helices with about four residues per turn in the central helical sections with the nonpolar residue side chains forming a hydrophobic face inside a triple superhelix. The nine helical segments of the 19 kDa protein were modeled into three sets of three interacting coiled-coil helices with segments positioned end to end. The resulting structure lengthens with the addition of the N- and C-terminal sections, to give an axial ratio of approximately 6 or 7:1 in agreement with recent experiments. The natural carotenoid, lutein, is found to fit into the core of the triple-helical segments and help stabilize the configuration. Molecular dynamics simulations with explicit methanol/water molecules as solvent have been carried out to refine the 3D structure.

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