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Showing 1 to 4 of 4 for “"protein hydrophobicity"”.

  1. Intrinsically Disordered Protein Polymer Libraries as Tools to Understand Protein Hydrophobicity

    <p>Intrinsically disordered protein polymers (IDPPs) are repetitive biopolymers that, when enriched with prolines, glycines, and aliphatic amino acids, have observable lower critical solution temperature (LCST) phase transition behavior at physiologically relevant temperature and concentration …

    duke Repository record for Intrinsically Disordered Protein Polymer Libraries as Tools to Understand Protein Hydrophobicity (opens in a new tab)

  2. The Effect of Stability and Surface Charge Distribution on Secretion of Bovine Pancreatic Trypsin Inhibitor From Yeast

    … results in a dramatic increase in the relative hydrophobicity of the molecule, compared to removal of other charges. On the basis of these data, we suggest that the ER acts as a cation exchange column and that the ER quality control apparatus decreases the yield of proteins with longer ER …

    uiuc Repository record for The Effect of Stability and Surface Charge Distribution on Secretion of Bovine Pancreatic Trypsin Inhibitor From Yeast (opens in a new tab)

  3. Aspects of bioorganic chemistry - a). Development of caffeine-aptamer for coffee decaffeination; b). Study of 1,8-naphthalimide derivatives as fluorescent probes; c). Encapsulation of DNA by silica nanoparticles

    … stain biomolecules based on differences in their hydrophobicity. 1,8-naphthalimide derivatives were synthesized, and their photophysical and staining properties were investigated. The fluorescence intensity of 4-phenyl-1,8-naphthalimide was found to be very sensitive to solvent polarity, where the …

    brock Repository record for Aspects of bioorganic chemistry - a). Development of caffeine-aptamer for coffee decaffeination; b). Study of 1,8-naphthalimide derivatives as fluorescent probes; c). Encapsulation of DNA by silica nanoparticles (opens in a new tab)

  4. INTERACTION BETWEEN PROTEINS OF PLANT ORIGIN AND WINE COMPONENTS: MOLECULAR-BASED CHOICE OF PROTEIN FINING AGENTS FOR ORGANOLEPTIC IMPROVEMENT

    … casein, egg albumin, and, more recently, proteins from plant sources are commonly used in winemaking as fining agents to remove particles responsible for turbidity, to improve stability, and to control browning, over-oxidation, and bitterness during ageing (Spagna et al., 2000; Cosme et …

    milano Repository record for INTERACTION BETWEEN PROTEINS OF PLANT ORIGIN AND WINE COMPONENTS: MOLECULAR-BASED CHOICE OF PROTEIN FINING AGENTS FOR ORGANOLEPTIC IMPROVEMENT (opens in a new tab)