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operation and life. The collisional plasma will also tend to have a low electron temperature, which reduces the sheath voltages and further protects the low work function insert surface from damage or modification by the plasma. It is possible to describe [26] the insert plasma using simple particle and energy balance models and plasma diffusion models because the plasma transport inside the hollow cathode is dominated by collisions. In 3, the solution to the radial diffusion equation for ions in collisionally dominated plasmas in cylindrical geometry resulted in an eigenvalue equation with a unique dependence on the electron temperature: (6.4- 1) where R is the internal radius of the insert, is the first zero of the zero-order Bessel function, no is the neutral (density, oi is the ionization cross section averaged over a Maxwellian electron temperature, and D is the diffusion coefficient. This means that the electron temperature is constrained to produce sufficient ions to offset the diffusion losses to the wall. The diffusion in the radial direction. in the insert region is ambipolar, and the ion mobility is limited by resonant charge exchange (CEX) with the xenon neutral atoms. The average collisions frequency for the ions is then



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The FileMaker Pro menu system provides users with access to all the basic application features and functions, but it does so in a generic way without reference to the particular needs, habits, preferences, or vocabulary of your users. You can improve your solutions usability by modifying the menus to remove commands not required by your users, to rename commands so that their meaning is specific to your solution (for example, New Contact instead of New Record ), and/or to change the way commands operate, according to the needs of your users.

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which is derived by simple arithmetic manipulation from Equation (8.33). Where unambiguous cooperative biocatalysis is taking place, then a plot of values of log( /Vmax ) versus log[S] should render a straight line of slope n (Figure 8.32). In principle, all single-substrate multi-subunit/multi-catalytic-site biocatalysts may be subject to positive cooperativity in catalysis under certain conditions according to Equation (8.34). The single-substrate multi-subunit/multi-catalytic-site biocatalyst is almost designed for this opportunity. However, as we have seen already this opportunity need not be taken advantage of for a given single-substrate biocatalyst operating in a given catalytic niche. Also, positive cooperativity does not necessarily have to be a subject to substrate binding. For instance, pH changes may induce cooperative shifts in catalytic behaviour of a single-substrate biocatalyst such as the homo-hexameric E. coli GadB enzyme responsible for -decarboxylation of glutamate to give carbon dioxide and -amino butyric acid (GABA) (Figure 8.5, Table 8.1). In this case, Equation (8.34) needs to be modi ed so that [H+ ] replaces [S] to re ect the actual single participant in this positive cooperative process. The effect of increasing [H+ ] is to promote a rapid and substantial conformational change within the homohexameric enzyme structure, leading to transition from the inactive form (T state) of the enzyme at

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