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  • 1
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 91 (1989), S. 7557-7562 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: The rate of intramolecular electronic excitation energy transfer in 9,9' bifluorene has been investigated in a variety of solvents, using both time-correlated single photon counting and femtosecond fluorescence upconversion technique. The kinetics of energy transfer were determined in both cases by time dependent fluorescence anisotropy measurements. The energy transfer dynamics between fluorene moieties has been found to occur on a time scale of approximately 600 fs in different solvents and has been correlated with the T2 value calculated from the absorption linewidth and the β value obtained from jet measurements. The dihedral angle between the fluorene moieties was also calculated from the anisotropy measurement and compared with the values obtained from a solution phase NMR determination.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of food science & technology 38 (2003), S. 0 
    ISSN: 1365-2621
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Cryoprotection of protein by highly concentrated branched oligosaccharides (HBOS) was investigated by using a model solution containing bovine serum albumin (BSA). The glass transition temperature of the BSA solution with HBOS, determined by modulated differential scanning calorimetry, was −16.1 °C, which is higher than that of sucrose at either 4 or 8% concentration by weight (−27.2 °C). Also, changes in the unfrozen water fraction and their mobilities, determined by nuclear magnetic resonance, were used as indices of protein stabilization. The results revealed that the amount of unfrozen water increased whereas the mobility was decreased by addition of HBOS. Thus we propose that the cryoprotection effect can occur by preserving the protein in a rigid structure formed by the water and the cryoprotectant HBOS.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 97 (1992), S. 4421-4427 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: Femtosecond infrared coherent transients have been measured for the stretch vibration of CO on Cu(111). The free induction decay exhibits a dephasing time (T2) of 2±0.3 ps (and 2±0.1 ps assuming a single exponential decay between 2 and 3 ps). The decay was best fit by exponential relaxation, thereby suggesting that the CO vibrational band is almost entirely homogeneously broadened. The surface sum frequency spectrum was also measured at two coverages (0.10 and 0.45 L) using spectrally narrowed pulses. Interferences were observed leading to a determination of the relative phase and amplitude of the resonant and nonresonant second-order susceptibility in this system. The magnitude of the nonresonant susceptibility was only weakly dependent on coverage, suggesting that the nonresonant polarizability originates in the bulk Cu. Time and frequency domain results were in good agreement.
    Type of Medium: Electronic Resource
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