Repulsion motor

Repulsion Motor. A repulsion motor is a single-phase motor that has a stator winding arranged h)r connection to a commutator. Brushes on the commutator are short circuited and are so placed that the magnetic axis of the stator winding. This type of motor has a varying-speed characteristic. 

Repulsion-Start Induction Motor. A repulsion-start induction motor is a single-pliasc motor having the same windings as a repulsion motor, but at a predetermined speed the rotor winding is short circuited or otherwise connected to give the equivalent of a squirrel-cage winding. This type of motor starts as a repulsion motor but operates as an induction motor w ith constant-speed characteristics. 

Repulsion-Induction Motor. A repulsion-induction motor is a form of repulsion motor that has a squirrel-cage winding in the rotor in addition to the repulsion motor w inding. A motor of this type may have either a constant-speed (see MG 1-1.30) or varying-speed (.see MG 1-1.31) characteristic. 

FIGURE 5.108 Schematic and speed vs. torque diagram—ac repulsion motor. 

Repulsion-Start Motors. Repulsion-start motors are repulsion motors with a centrifugal switch (Fig. 5.109). At about 75 percent of synchronous speed, the switch short-circuits the commutator bars and the motor performs hke a squirrel-cage motor. Repulsion-start motors are expensive and no longer widely used in indust. ... 

The attraction and repulsion between the poles on the rotor and stator cause the electromagnet to rotate. Direct-current motors usually need commutators to achieve continuous motion. 

Multiparticle collision dynamics provides an ideal way to simulate the motion of small self-propelled objects since the interaction between the solvent and the motor can be specified and hydrodynamic effects are taken into account automatically. It has been used to investigate the self-propelled motion of swimmers composed of linked beads that undergo non-time-reversible cyclic motion [116] and chemically powered nanodimers [117]. The chemically powered nanodimers can serve as models for the motions of the bimetallic nanodimers discussed earlier. The nanodimers are made from two spheres separated by a fixed distance R dissolved in a solvent of A and B molecules. One dimer sphere (C) catalyzes the irreversible reaction A + C B I C, while nonreactive interactions occur with the noncatalytic sphere (N). The nanodimer and reactive events are shown in Fig. 22. The A and B species interact with the nanodimer spheres through repulsive Lennard-Jones (LJ) potentials in Eq. (76). The MPC simulations assume that the potentials satisfy Vca = Vcb = Vna, with c.,t and Vnb with 3- The A molecules react to form B molecules when they approach the catalytic sphere within the interaction distance r < rc. The B molecules produced in the reaction interact differently with the catalytic and noncatalytic spheres. 

The necessity for an instantaneous tripping function is the same as for a high voltage motor. This function can be provided by a magnetic repulsion device within the moulded case circuit breaker, by a (50) relay or by upstream fuses. If fuses are used then the contactor must be capable of carrying the duty until the fuse completes its function. To minimise the stressing of the contactor it should be coordinated with the fuses as recommended in IEC60947 Part 2, as a Type 2 requirement. 

Split-phase Repulsion-stait induction CqKidnnr-stait r- R ulsion-induction Cq>acitor-motor... 

When the space-filling protein component is removed, it becomes possible to view the located water molecules within the myosin motor. As shown in Figure 1.5B, an impressive number and distribution of the detected water molecules appear. It can also be expected that there are many more water molecules relevant to function of the myosin motor that are too mobile to be seen by X-ray diffraction, just as is apparent in the crevices and recesses of the surface. By the consilient mechanism these water molecules (seen in Fig. 1.5B and the additional unseen water molecules) are essential to motor function. These water molecules, which in our view are essential for Life, we choose to call the waters of Thales. Thus, as required for this protein motor to function by the consilient mechanism, internal water molecules do exist. Accordingly, in our view, this fundamental protein motor that produces motion contains ample water as part of the structure in order to function in the competition for water between oil-like and vinegar-like groups, which competition expresses as a repulsion between these groups. 

D.W. Urry, Function of the Fi-motor (Fi-ATPase) of ATP synthase by Apolar-polar Repulsion through Internal Interfacial Water. Cell Biol. Int., 33(1), 44-55,2006. 

The Fo-motor presents a simplistic utilization of the consilient mechanism. The repulsion, between a vinegar-like carboxylate of a cleat of a wheel and the sea of oil of a cell membrane, becomes an attraction on protonation, and the wheel rotates one cleat into the oily membrane as a second cleat rotates into a sufficiently polar/aqueous position for a carboxyl to release its proton to the other side of the membrane. The direction of rotation of the wheel and importantly of the axle (the y-rotor) that extends from the wheel depends on the frequency with which protons enter and leave from each side of the membrane. This straightforward demonstration of the consilient mechanism will be considered in more detail in relation to Figures 8.26 through 8.30. 

The Fi-motor ATP Synthesis by Changing Repulsion Between the Oil-like Surface of the Rotor and the Charged Nucleotides at the Origin of Water-filled Clefts... 

The same repulsive interaction, AGap, between an oU-like surface and charges associated with the nucleotides occurs in the synthesis of ATP from ADP and Pj by the Fi-motor— the second, the extramembrane, component of ATP synthase. As noted above, the intramembrane component functions to rotate an axle-like projection, called the y-rotor, from the center of an intramembrane rotary motor driven by protons. 

Figure 2.13. Shown is one complete cycle of the Fj-motor of ATP synthase on filling all catalytic sites with nucleotide and with a y-rotor that has three faces of very different hydrophobicities, that is, of very different oil-like character. As discussed in Chapter 8, the relative oil-like character of the three faces compare as -20kcal/mol-face for the most oillike, -i-Okcal/mol-face for an essentially neutral face, and h-9 kcal/mol-face for the least oil-like face. The least oil-like face would allow ADP and Pi to enter the catalytic site. As the Fo-motor rotates the darkened, oil-like face of the rotor toward the catalytic site containing ADP plus Pi, the repulsion between...

In Chapter 8, more structural background and molecular details of contraction exhibited by the linear myosin II motor are considered after, in Chapter 5, the physical basis for the apolar (oil-like)-polar (vinegar-like) repulsive energy that controls hydrophobic association is experimentally and analytically developed. The crystal structures of the cross-bridge of scallop muscle provide remarkable examples of the consilient mechanism functioning in this protein-based machine ... 

The multivalent phosphates, already significantly limited in hydration, can be expected to reach out substantially further than carboxylates in their search for adequate hydration. This effect becomes enhanced when phosphate access to water is limited. When the phosphate occurs at the base of a cleft, the direction for access of water becomes severely limited and the thirst for hydration can be directed by the cleft to target sites of hydrophobic association. In other words, the cleft functions as a conduit to direct the thirst for hydration. By means of the cleft, the capacity for disrupting hydrophobic hydration to target sites can be boosted by effecting separation of ion pairs enroute, which boost the polar species capacity to disrupt hydrophobic hydration. Accordingly, the use of structure to direct the forces of apolar-polar repulsion becomes a useful design feature in certain ATP-driven protein-based machines, such as the myosin II motor. 

As discussed below in section 8.4.4.11, ATP binding provides the major push component of force, but we expect the peak in AG.p to occur at the moment of hydrolysis when the charge concentration is greatest with the momentary presence of both ADP and Pj In the synthesis function of the Fi motor of ATP synthase, we expect that the maximum repulsion occurs between the most hydrophobic side of the rotor and the ADP and Pj state and that this maximal repulsion decreases on ATP formation, which, in the consiUent view, drives ATP formation. Accordingly, because repulsion is the force that drives the ATPase function of the Fi motor and because repulsion drives rotation, ATP binding would provide near-maximal force generation, enhanced only at the moment of hydrolysis to form ADP plus Pj. 

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