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  • 1
    Electronic Resource
    Electronic Resource
    Neutron reflectivity study of adsorbed diblock copolymers (1994)
    Springer
    Il nuovo cimento della Società Italiana di Fisica 16 (1994), S. 721-726 
    Details
    ISSN: 0392-6737
    Keywords: Neutron scattering techniques (including small-angle scattering) ; Macromolecular and polymer solutions (solubility, swelling, etc.) ; polymer melts ; Solid-fluid interfaces ; Structure and morphology ; thickness ; Conference proceedings
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Summary In this paper, we summarize our cumulative work on neutron reflectivity studies of polystyrene-poly(vinyl-2-pyridine) (PS-PVP) and polystyrene-polyethylene oxide (PS-PEO) adsorbed at a quartz-solvent interface. Deuterated toluene was chosen as the solvent since it is a good solvent for PS and a poor one for either of the other two blocks. In this case, the polystyrene dangles into the solvent while the other block acts as an anchor. The neutron reflectivity studies reveal that the form of the polymer density profile normal to the substrate may be varied from an extended «brush» to a condensed «mushroom» conformation by manipulating the ratio of the molecular weights of the two blocks. In addition, we present new data on the PS-PEO system in a poor solvent, deuterated cyclohexane, under conditions of shear flow in Poiseuille geometry. We find that when the PS-PEO diblock is absorbed from cyclohexane and is allowed to relax, the PS chain takes on a «mushroom» conformation. However, when the shear is applied, the layer shear thickens due to the PS chains extending to nearly twice their original lengths.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02456717
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  • 2
    Electronic Resource
    Electronic Resource
    The purification and characterization of homologous high molecular weight storage proteins from grain of wheat, rye and barley (1982)
    Springer
    Theoretical and applied genetics 62 (1982), S. 329-336 
    Details
    ISSN: 1432-2242
    Keywords: HMW storage prolamins ; Wheat ; Rye ; Barley ; Characterization and purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Homologous high molecular weight storage prolamins were purified from grain of wheat, rye and barley using combinations of gel filtration, ion-exchange chromatography and preparative isoelectric focusing. Sodium dodecylsulphate polyacrylamide gel electrophoresis showed that the components were single bands with apparent mol.wts. of above 100,000. Molecular weights determined by sedimentation equilibrium ultracentrifugation were considerably lower; 54,700, 67,600 and 69,600 for the components from barley, rye and wheat respectively. Amino acid analysis showed the presence of 13.6 to 16.5 mol% glycine, 29.6 to 34.0 mol% glutamate + glutamine, 11.4 to 13.7 mol% proline and a total of 4.0 to 5.7 mol% basic amino acids. Automated N-terminal amino acid sequencing of the component from wheat showed the presence of cysteine residues at positions 5 and 10, and this is discussed in relation to the possible role of these proteins in the visco-elastic gluten network.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00275097
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  • 3
    Electronic Resource
    Electronic Resource
    Analysis of HMW glutenin subunits encoded by chromosome 1A of bread wheat (Triticum aestivum L.) indicates quantitative effects on grain quality (1992)
    Springer
    Theoretical and applied genetics 83 (1992), S. 373-378 
    Details
    ISSN: 1432-2242
    Keywords: Wheat ; HMW glutenin subunits ; Bread-making quality ; Gene ; Protein sequence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A gene encoding the high-molecular-weight (HMW) subunit of glutenin 1Ax1 was isolated from bread wheat cv Hope. Comparison of the deduced amino acid sequence with that previously reported for an allelic subunit, 1Ax2*, showed only minor differences, which were consistent with both subunits being associated with good bread-making quality. Quantitative analyses of total protein extracts from 22 cultivars of bread wheat showed that the presence of either subunit 1Ax1 or 1Ax2*, when compared with a null allele, resulted in an increase in the proportion of HMW subunit protein from ca. 8 to 10% of the total. It is suggested that this quantitative increase in HMW subunit protein may account for the association of 1Ax subunits with good quality.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00224285
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