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Fractional dynamical importance

The fractional dynamical importance of the /c- th resonance operator relative to all of the coupling terms in Hres is... [Pg.649]

This theorem is of fundamental importance in fractional dynamics because use of it coupled with continued fraction methods [8] allows recurrence relations associated with normal diffusion to be generalized to fractional dynamics in an obvious fashion.) Regarding the ac response, if we assume that the above result may be analytically continued into the domain of the imaginaries or if we equivalently note that if D denotes the operator d/dt and G(oo) denotes an arbitrary function of oo, then [42]... [Pg.309]

Relaxation functions for fractal random walks are fundamental in the kinetics of complex systems such as liquid crystals, amorphous semiconductors and polymers, glass forming liquids, and so on [73]. Relaxation in these systems may deviate considerably from the exponential (Debye) pattern. An important task in dielectric relaxation of complex systems is to extend [74,75] the Debye theory of relaxation of polar molecules to fractional dynamics, so that empirical decay functions for example, the stretched exponential of Williams and Watts [76] may be justified in terms of continuous-time random walks. [Pg.176]

In the optical bands, thousands of individual knots have been observed to yield kinematic information, whereas the X-rays probe more dynamically important information since a much larger fraction of the ejecta mass is probed by X-rays... [Pg.262]

The secondary and tertiary structures of myoglobin and ribonuclease A illustrate the importance of packing in tertiary structures. Secondary structures pack closely to one another and also intercalate with (insert between) extended polypeptide chains. If the sum of the van der Waals volumes of a protein s constituent amino acids is divided by the volume occupied by the protein, packing densities of 0.72 to 0.77 are typically obtained. This means that, even with close packing, approximately 25% of the total volume of a protein is not occupied by protein atoms. Nearly all of this space is in the form of very small cavities. Cavities the size of water molecules or larger do occasionally occur, but they make up only a small fraction of the total protein volume. It is likely that such cavities provide flexibility for proteins and facilitate conformation changes and a wide range of protein dynamics (discussed later). [Pg.181]

Under changing flow conditions, it can be important to include some consideration of the hydrodynamic changes within the column (Fig. 3.53), as manifested by changes in the fractional dispersed phase holdup, h , and the phase flow rates, Ln and G . which, under dynamic conditions, can vary from stage to stage. Such variations can have a considerable effect on the overall dynamic characteristics of an extraction column, since variations in hn also... [Pg.195]

Lipid-protein interactions are of major importance in the structural and dynamic properties of biological membranes. Fluorescent probes can provide much information on these interactions. For example, van Paridon et al.a) used a synthetic derivative of phosphatidylinositol (PI) with a ris-parinaric acid (see formula in Figure 8.4) covalently linked on the sn-2 position for probing phospholipid vesicles and biological membranes. The emission anisotropy decays of this 2-parinaroyl-phosphatidylinositol (PPI) probe incorporated into vesicles consisting of phosphatidylcholine (PC) (with a fraction of 5 mol % of PI) and into acetylcholine receptor rich membranes from Torpedo marmorata are shown in Figure B8.3.1. [Pg.243]

The extent to which ions, etc. adsorb or experience an electrostatic ( coulombic ) attraction with the surface of an electrode is determined by the material from which the electrode is made (the substrate), the chemical nature of the materials adsorbed (the adsorbate) and the potential of the electrode to which they adhere. Adsorption is not a static process, but is dynamic, and so ions etc. stick to the electrode (adsorb) and leave its surface (desorb) all the time. At equilibrium, the rate of adsorption is the same as the rate of desorption, thus ensuring that the fraction of the electrode surface covered with adsorbed material is constant. The double-layer is important because faradaic charge - the useful component of the overall charge - represents the passage of electrons through the double-layer to effect redox changes to the material in solution. [Pg.117]


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Fractional dynamics

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