Interactions of alcohols with soy protein isolate were investigated using an equilibrium dialysis method. It was found that interactions may involve hydrophobic association and, to some degree, hydrogen bonding. Studies with soy protein with various levels of denaturation indicated that denaturation of the protein by heating may limit its ability for the formation of hydrogen bonds with alcohols. The proteins under investigation exhibited practically unlimited binding capacity for alcohols.
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AbstractIn this paper we introduce data characterizations for fitting chaotic data to linear combinations of one-dimensional maps (say, of the unit interval) for use in subgrid-scale turbulence models. We test the efficacy of these characterizations on data generated by a chaotically-forced Burgers' equation and demonstrate, very satisfactory results in terms of modeIed time series, power spectra and delay maps.
DECLAIMER
DISCLAIMERPortions of this document may be illegible in electronic image products. Images are produced from the best available original document.
AbstractIn this paper we introduce data characterizations for fitting chaotic data to linear combinations of one-dimensional maps (say, of the unit interval) for use in subgrid-scale turbulence models. We test the efficacy of these characterizations on data generated by a chaotically-forced Burgers' equation and demonstrate, very satisfactory results in terms of modeIed time series, power spectra and delay maps.
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