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  • activity coefficients  (1)
  • equilibrium unfolding  (1)
  • potassium bromide  (1)
  • 1
    ISSN: 1572-8927
    Keywords: Isothermal diffusion ; diffusion coefficients ; aqueous solution ; ternary system ; Bu4NBr ; HBr ; primary charge effect ; activity coefficients
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Four diffusion coefficients for one composition of the system H2O-Bu4NBr-HBr were obtained at 25°C. The value of (D 12)v was negative and large as expected from the primary charge effect. However, the value of (D 21)v was also negative despite the fact that the primary charge effect predicts a positive value. This was interpreted to be a consequence of a large negative value for δ ln y2/δC1 which overshadows the primary charge effect.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-8927
    Keywords: Isothermal diffusion ; aqueous solution ; ternary system ; tetrabutylammonium bromide ; potassium bromide ; ionic transport coefficients ; water structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Sets of four diffusion coefficients were obtained for the water-tetrabutylammonium bromide-potassium bromide system at 25°C as a function of tetrabutylammonium bromide concentration with the mean concentration of potassiumbromide fixed at 0.1 mole-liter−1. The experiments were performed at tetrabutylammonium bromide concentrations of 0.075, 0.15, 0.3, and 0.45 mole-liter−1. The results are compared with the binary diffusion coefficients of these components and also with the calculated diffusion coefficients using the first approximation theory.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 15 (1996), S. 731-736 
    ISSN: 1573-4943
    Keywords: Mutant ribose-binding protein ; equilibrium unfolding ; refolding kinetics ; domain folding
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract A mature mutant ribose-binding protein (RBP) ofEscherichia coli was obtained by site-directed mutagenesis, replacing Thr-3 in the N-domain of wild-type mature RBP (WT-mRBP) with a Trp residue (N-Trp-mRBP). The equilibrium unfolding properties and the refolding kinetics of this protein were monitored by fluorescence and circular dichroism (CD). The stability of N-Trp-mRBP appears to be the same as that of C-Trp-mRBP, another mutant obtained by replacing Phe-187 with a Trp, and lower than that of WT-mRBP. The overall refolding rate of N-Trp-mRBP is much smaller than that of C-Trp-mRBP, which, in turn, is similar to that of WT-mRBP. For the case of WT-mRBP, the rate constant obtained by Tyr fluorescence is identical to the value obtained by CD. But with C-Trp-mRBP, the rate constant from CD is smaller than the value from the Trp fluorescence and this difference in the rate constants is much greater with the N-TrpmRBP.
    Type of Medium: Electronic Resource
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