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Stability diagram cross-section

The nonlinear modes are usually referred to as solutions to the nonlinear Helmholtz equation in the waveguide cross-section. For their investigation, power-dispersion diagrams are commonly used that give values of critical powers and are helpful in stability analysis of the fundamental mode. ... [Pg.157]

Figure 1. Schematic diagram showing the possible mechanisms of thin film stabilization, (a) The Marangoni mechanism in surfactant films (b) The viscoelastic mechanism in protein-stabilized films (c) Instability in mixed component films. The thin films are shown in cross section and the aqueous interlamellar phase is shaded. Figure 1. Schematic diagram showing the possible mechanisms of thin film stabilization, (a) The Marangoni mechanism in surfactant films (b) The viscoelastic mechanism in protein-stabilized films (c) Instability in mixed component films. The thin films are shown in cross section and the aqueous interlamellar phase is shaded.
Fig. 7.2. Developmental path of the cAMP signaUing system in the parameter space formed by adenylate cyclase and phosphodiesterase activity. The stability diagram is established by linear stability analysis of the steady state admitted by the three-variable system (5.1) governing the dynamics of the allosteric model for cAMP signalling in D. discoideum (see section 5.2). In domain C sustained oscillations occur around an unstable steady state. In domain B, the steady state is stable but excitable as it amplifies in a pulsatile manner a suprathreshold perturbation of given amplitude. Outside these domains the steady state is stable and not excitable. The arrow crossing successively domains A, B and C represents the developmental path that the system should follow in that parameter space to account for the observed sequence of developmental transitions no relay relay oscillations (Goldbeter, 1980). Fig. 7.2. Developmental path of the cAMP signaUing system in the parameter space formed by adenylate cyclase and phosphodiesterase activity. The stability diagram is established by linear stability analysis of the steady state admitted by the three-variable system (5.1) governing the dynamics of the allosteric model for cAMP signalling in D. discoideum (see section 5.2). In domain C sustained oscillations occur around an unstable steady state. In domain B, the steady state is stable but excitable as it amplifies in a pulsatile manner a suprathreshold perturbation of given amplitude. Outside these domains the steady state is stable and not excitable. The arrow crossing successively domains A, B and C represents the developmental path that the system should follow in that parameter space to account for the observed sequence of developmental transitions no relay relay oscillations (Goldbeter, 1980).
FIGURE 11.16 Cross-section of the stability diagram for different values of V. The canyon... [Pg.351]

Fig. 55. P-T cross section of the pseudo-binary P-T-x phase diagram of 123-Oj. The stability field of the 123 phase is smaller than shown. Slow decomposition kinetics do not allow the exact determination of the phase boundary with the 124 phase. After Karpinsid et al. (1991). Fig. 55. P-T cross section of the pseudo-binary P-T-x phase diagram of 123-Oj. The stability field of the 123 phase is smaller than shown. Slow decomposition kinetics do not allow the exact determination of the phase boundary with the 124 phase. After Karpinsid et al. (1991).
Fig. 5 A diagram of a beta-hairpin molecule, showing the hydrogen bonds dotted lines) that stabilize the folded conformation between carboxyl and amide groups [28], On folding, the hydrophobic, valine side chain-rich face collapses together with a neighbor to form a bilayered fibril cross-section. The hairpins also hydrogen bond with neighbors to form fibrils that branch and entangle with physical crosslinks as indicated by the arrows in the Cryo-TEM image [49]... Fig. 5 A diagram of a beta-hairpin molecule, showing the hydrogen bonds dotted lines) that stabilize the folded conformation between carboxyl and amide groups [28], On folding, the hydrophobic, valine side chain-rich face collapses together with a neighbor to form a bilayered fibril cross-section. The hairpins also hydrogen bond with neighbors to form fibrils that branch and entangle with physical crosslinks as indicated by the arrows in the Cryo-TEM image [49]...

See other pages where Stability diagram cross-section is mentioned: [Pg.174]    [Pg.52]    [Pg.289]    [Pg.326]    [Pg.179]    [Pg.281]    [Pg.29]    [Pg.396]    [Pg.140]    [Pg.350]    [Pg.153]    [Pg.378]    [Pg.37]    [Pg.326]    [Pg.272]    [Pg.12]    [Pg.275]    [Pg.244]    [Pg.414]    [Pg.202]   
See also in sourсe #XX -- [ Pg.351 ]




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