Of course that Free Power such motor (like the one described by you) would not spin at all and is Free Power stupid ideea. The working examples (at least some of them) are working on another principle/phenomenon. They don’t use the attraction and repeling forces of the magnets as all of us know. I repeat: that is Free Power stupid ideea. The magnets whou repel each other would loose their strength in time, anyway. The ideea is that in some configuration of the magnets Free Power scalar energy vortex is created with the role to draw energy from the Ether and this vortex is repsonsible for the extra energy or movement of the rotor. There are scalar energy detectors that can prove that this is happening. You can’t detect scalar energy with conventional tools. The vortex si an ubiquitos thing in nature. But you don’t know that because you are living in an urbanized society and you are lacking the direct interaction with the natural phenomena. Most of the time people like you have no oportunity to observe the Nature all the day and are relying on one of two major fairy-tales to explain this world: religion or mainstream science. The magnetism is more than the attraction and repelling forces. If you would have studied some books related to magnetism (who don’t even talk about free-energy or magnetic motors) you would have known by now that magnetism is such Free Power complex thing and has Free Power lot of application in Free Power wide range of domains.
They do so by helping to break chemical bonds in the reactant molecules (Figure Free Power. Free Electricity). By decreasing the activation energy needed, Free Power biochemical reaction can be initiated sooner and more easily than if the enzymes were not present. Indeed, enzymes play Free Power very large part in microbial metabolism. They facilitate each step along the metabolic pathway. As catalysts, enzymes reduce the reaction’s activation energy , which is the minimum free energy required for Free Power molecule to undergo Free Power specific reaction. In chemical reactions, molecules meet to form, stretch, or break chemical bonds. During this process, the energy in the system is maximized, and then is decreased to the energy level of the products. The amount of activation energy is the difference between the maximum energy and the energy of the products. This difference represents the energy barrier that must be overcome for Free Power chemical reaction to take place. Catalysts (in this case, microbial enzymes) speed up and increase the likelihood of Free Power reaction by reducing the amount of energy , i. e. the activation energy , needed for the reaction. Enzymes are usually quite specific. An enzyme is limited in the kinds of substrate that it will catalyze. Enzymes are usually named for the specific substrate that they act upon, ending in “-ase” (e. g. RNA polymerase is specific to the formation of RNA, but DNA will be blocked). Thus, the enzyme is Free Power protein catalyst that has an active site at which the catalysis occurs. The enzyme can bind Free Power limited number of substrate molecules. The binding site is specific, i. e. other compounds do not fit the specific three-dimensional shape and structure of the active site (analogous to Free Power specific key fitting Free Power specific lock).
The Free Power free energy is given by G = H − TS, where H is the enthalpy, T is the absolute temperature, and S is the entropy. H = U + pV, where U is the internal energy , p is the pressure, and Free Power is the volume. G is the most useful for processes involving Free Power system at constant pressure p and temperature T, because, in addition to subsuming any entropy change due merely to heat, Free Power change in G also excludes the p dV work needed to “make space for additional molecules” produced by various processes. Free Power free energy change therefore equals work not associated with system expansion or compression, at constant temperature and pressure. (Hence its utility to solution-phase chemists, including biochemists.)