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  • 1
    ISSN: 1572-8927
    Keywords: Partial molar isentropic pressure coefficient ; speed of sound ; dipeptide ; aqueous solution ; side chain solvation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The partial molar isentropic pressure coefficients at infinite dilution, K S,2 o , have been determined for a number of dipeptides in aqueous solution at 25°C. For a series of dipeptides of sequence gly-X, where X is an amino acid with a neutral side chain, the K S,2 o values are all more negative than that for diglycine. The results are discussed in terms of the hydration of the side chains. There are significant differences in the K S,2 o values for sequence isomeric dipeptides. These differences can be rationalized in terms of the mutual interactions between the side chain and the ionic end groups in the dipeptides. Possible relationships between K S,2 o and V 2 o , the partial molar volume at infinite dilution, were investigated. For the dipeptides of sequence gly-X there is an interesting linear relationship between K S,2 o /V 2 o and V 2 o .
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1572-8927
    Keywords: Partial molar isentropic compressibility ; temperature dependence ; speed of sound ; dipeptide ; aqueous solution
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The partial molar isentropic compressibilities at infinite dilution,K s,2 o , have been obtained for eight glycyl dipeptides of sequence gly-X (X is an amino acid) in aqueous solution at the temperatures 15 and 35°C. The results have been combined with those obtained at 25°C, that were reported earlier, to evaluate the temperature dependences ofK s,2 o for the dipeptides in the temperature range 15 to 35°C. TheK s,2 o values for all the dipeptides are negative and increase (become more positive) with an increase in temperature. The slopes of the temperature dependences ofK s,2 o for the dipeptides with typically hydrophobic side-chains are significantly larger than those for dipeptides with hydrophilic side-chains.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1572-8927
    Keywords: Stability constants ; partial molal volume ; isentropic partial molal compressibility ; ionic partial molal compressibility ; complex formation ; crown ether ; cations ; water ; hydration number ; electrostriction ; scaled particle theory ; intrinsic volume ; Drude-Nernst continuum model
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The stability constants and the partial molal volume and isentropic partial molal compressibility changes of complex formation between cations and crown ethers in water at 25°C are presented. The cations involved are Na+, K+, Rb+, Cs+, Ca2+, and Ba2+, and the crown ethers are 12-crown-4, 15-crown-5, and 18-crown-6. Values of ΔV of complex formation have been discussed in terms of two simple models, one based on the scaled particle theory, and the others on the Drude-Nernst continuum model. The results indicate that the charge of the potassium cation in 18-crown-6 is especially well screened from the water. On this basis hydration numbers of complexed cations have been calculated. This shows that the size of the cation compared to the crown ether hole is important for the contacts between complexed cations and water.
    Type of Medium: Electronic Resource
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