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Intensity viscosity dependence

Dynamic quenching of fluorescence is described in Section 4.2.2. This translational diffusion process is viscosity-dependent and is thus expected to provide information on the fluidity of a microenvironment, but it must occur in a time-scale comparable to the excited-state lifetime of the fluorophore (experimental time window). When transient effects are negligible, the rate constant kq for quenching can be easily determined by measuring the fluorescence intensity or lifetime as a function of the quencher concentration the results can be analyzed using the Stern-Volmer relation ... [Pg.232]

How does solvent viscosity depend on temperature How can that affect signal intensity in a pulsed experiment ... [Pg.104]

Optical temperature sensor (opt(r)odes) based on the viscosity-dependent intramolecular excimer formation of l,3bi(l-pyrenyl)propane in [C4mypr][Tf2N] have been developed [33], The relative intensity of the excimer emission was found to gain in intensity with higher temperature. This has been attributed to the generally low viscosity of the ionic liquid. The working temperature of this luminescence thermometer is between 25°C and about 150°C. [Pg.292]

Fig. 9 Viscosity dependence of TICT emission intensity. Sample I at 25°C. The line uaiJrawn by computer fitting,... Fig. 9 Viscosity dependence of TICT emission intensity. Sample I at 25°C. The line uaiJrawn by computer fitting,...
The interfacial rheology of protein adsorption layers has been intensively studied in relation to the properties of foams and emulsions stabilized by proteins and their mixtures with lipids or surfactants. Detailed information on the investigated systems, experimental techniques, and theoretical models can be found in Refs. [762-769]. The shear rheology of the adsorption layers of many proteins follows the viscoelastic thixotropic model [770-772], in which the surface shear elasticity and viscosity depend on the surface shear rate. The surface rheology of saponin adsorption layers has been investigated in Ref. [773]. [Pg.359]

The temperature dependence of fluorescence shows that tram cis photoisomerization as a competing path is activated the activation energy (Ej ,) lies in the 15-30 kj mol range (Table 36.2). The viscosity dependence of intensively studied by picosecond laser spectroscopy. 2 The relaxation rates of... [Pg.715]

The quantity k is related to the intensity of the turbulent fluctuations in the three directions, k = 0.5 u u. Equation 41 is derived from the Navier-Stokes equations and relates the rate of change of k to the advective transport by the mean motion, turbulent transport by diffusion, generation by interaction of turbulent stresses and mean velocity gradients, and destmction by the dissipation S. One-equation models retain an algebraic length scale, which is dependent only on local parameters. The Kohnogorov-Prandtl model (21) is a one-dimensional model in which the eddy viscosity is given by... [Pg.102]

Phloroglucinol is Hsted in the Colourindex as Cl Developer 19. It is particularly valuable in the dyeing of acetate fiber but also has been used as a coupler for azoic colors in viscose, Odon, cotton (qv), rayon, or nylon fibers, or in union fabrics containing these fibers (157). For example, cellulose acetate fabric is treated with an aromatic amine such as (9-dianisidine or a disperse dye such as A-hydroxyphenylazo-2-naphthylamine and the amine diazotizes on the fiber the fabric is then rinsed, freed of excess nitrite, and the azo color is developed in a phloroglucinol bath at pH 5—7. Depending on the diazo precursor used, intense blue to jet-black shades can be obtained with excellent light-, bleach-, and mbfastness. [Pg.384]

The mass-transfer coefficients depend on complex functions of diffii-sivity, viscosity, density, interfacial tension, and turbulence. Similarly, the mass-transfer area of the droplets depends on complex functions of viscosity, interfacial tension, density difference, extractor geometry, agitation intensity, agitator design, flow rates, and interfacial rag deposits. Only limited success has been achieved in correlating extractor performance with these basic principles. The lumped parameter deals directly with the ultimate design criterion, which is the height of an extraction tower. [Pg.1464]

The bubble size at formation varied with particle characteristics. It was further observed that the bubble size decreased with increasing fluidization intensity (i.e., with increasing liquid velocity). The rate of coalescence likewise decreased with increasing fluidization intensity the net rate of coalescence had a positive value at distances from 1 to 2 ft above the orifice, whereas at larger distances from the orifice the rate approached zero. The bubble rise-velocity increased steadily with bubble size in a manner similar to that observed for viscous fluids, but different to that observed for water. An attempt was made to explain the dependence of the rate of coalescence on fluidization intensity in terms of a relatively high viscosity of the liquid fluidized bed. [Pg.124]

Fig. 8. Dependence of (A) corrected diffusion coefficient (D), (B) steady-state fluorescence intensity, and (C) corrected number of particles in the observation volume (N) of Alexa488-coupled IFABP with urea concentration. The diffusion coefficient and number of particles data shown here are corrected for the effect of viscosity and refractive indices of the urea solutions as described in text. For steady-state fluorescence data the protein was excited at 488 nm using a PTI Alphascan fluorometer (Photon Technology International, South Brunswick, New Jersey). Emission spectra at different urea concentrations were recorded between 500 and 600 nm. A baseline control containing only buffer was subtracted from each spectrum. The area of the corrected spectrum was then plotted against denaturant concentrations to obtain the unfolding transition of the protein. Urea data monitored by steady-state fluorescence were fitted to a simple two-state model. Other experimental conditions are the same as in Figure 6. Fig. 8. Dependence of (A) corrected diffusion coefficient (D), (B) steady-state fluorescence intensity, and (C) corrected number of particles in the observation volume (N) of Alexa488-coupled IFABP with urea concentration. The diffusion coefficient and number of particles data shown here are corrected for the effect of viscosity and refractive indices of the urea solutions as described in text. For steady-state fluorescence data the protein was excited at 488 nm using a PTI Alphascan fluorometer (Photon Technology International, South Brunswick, New Jersey). Emission spectra at different urea concentrations were recorded between 500 and 600 nm. A baseline control containing only buffer was subtracted from each spectrum. The area of the corrected spectrum was then plotted against denaturant concentrations to obtain the unfolding transition of the protein. Urea data monitored by steady-state fluorescence were fitted to a simple two-state model. Other experimental conditions are the same as in Figure 6.

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See also in sourсe #XX -- [ Pg.145 ]




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