129 research outputs found

    Water Quality as Affected by Pesticides in Rice Production

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    Studies were conducted to determine the environmental persistence of the rice pesticides triclopyr, 2,4-D, benomyl and quinclorac. Triclopyr half-lives ranged from \u3c7 d to \u3e100 d depending on depth within the soil profile and clay content. Triclopyr persistence increased as depth within the profile increased and clay content increased. The benomyl metabolite MBC was present at greater than 50% of the initial amount after 9 months in the field. In simulated carryover field studies quinclorac exhibited the greatest potential for injury to subsequent rotational crops. Cotton and soybean growth was reduced when planted at four weeks after quinclorac application. The adsorption of triclopyr to three soils was measured by the batch equilibrium technique. Freundlich isotherms were linear and resulted in Kf values of 1.60, 1.41, and 2.75 for Crowley silt loam soil from depths of 0, 0.2, and 0.6 m, respectively, within soil profile. Soil thin-layer chromatography of triclopyr resulted in Rf values of 0.42, 0.69, and 0.40 for the Crowley silt loam soil from 0, 0.2, and 0.6 m depths. In controlled temperature and water potential degradation studies, triclopyr and 2,4-D degraded more rapidly at 3 0 C than at 15 C. The degradation rates of the two herbicides responded oppositely to water potential. 2,4-D degraded more rapidly under anaerobic conditions, whereas triclopyr degraded more rapidly under aerobic conditions

    Calculation of the Phase Behavior of Lipids

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    The self-assembly of monoacyl lipids in solution is studied employing a model in which the lipid's hydrocarbon tail is described within the Rotational Isomeric State framework and is attached to a simple hydrophilic head. Mean-field theory is employed, and the necessary partition function of a single lipid is obtained via a partial enumeration over a large sample of molecular conformations. The influence of the lipid architecture on the transition between the lamellar and inverted-hexagonal phases is calculated, and qualitative agreement with experiment is found.Comment: to appear in Phys.Rev.

    Single Honeybee Silk Protein Mimics Properties of Multi-Protein Silk

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    Honeybee silk is composed of four fibrous proteins that, unlike other silks, are readily synthesized at full-length and high yield. The four silk genes have been conserved for over 150 million years in all investigated bee, ant and hornet species, implying a distinct functional role for each protein. However, the amino acid composition and molecular architecture of the proteins are similar, suggesting functional redundancy. In this study we compare materials generated from a single honeybee silk protein to materials containing all four recombinant proteins or to natural honeybee silk. We analyse solution conformation by dynamic light scattering and circular dichroism, solid state structure by Fourier Transform Infrared spectroscopy and Raman spectroscopy, and fiber tensile properties by stress-strain analysis. The results demonstrate that fibers artificially generated from a single recombinant silk protein can reproduce the structural and mechanical properties of the natural silk. The importance of the four protein complex found in natural silk may lie in biological silk storage or hierarchical self-assembly. The finding that the functional properties of the mature material can be achieved with a single protein greatly simplifies the route to production for artificial honeybee silk

    Non-ionic Thermoresponsive Polymers in Water

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