FX chains

More than one effect can be used at a time on a single track, bus, or project. FX are applied in a particular order in an FX Chain. The order of plug-ins can be important in the final sound. Some FX belong very late in the chain (such as EQ and Reverb) and some earlier (Compression). Others shonld be used in a particular order. Track FX plug-ins are usually applied in this order Compression, Noise Gate, and, finally, EQ. This is not a hard and fast mle, and there may be creative reasons why you d want to alter this sequence. FX chains and ordering are discnssed in more detail in the next chapter. 

Three effects appUed in a chain to a track in the Audio Plug-In dialog. 

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Chuang et ai propose that the a chain (as well as the y chain) evolved from the (x chain, but that the a chain arose more recently. On the basis of the approximate rates of evolution of other immunoglobulin polypeptide chains they estimated that the a chain appeared about 200 X 10 years ago. This would be consistent with its presence in birds and animals and its (presumed) absence in reptiles, amphibia, and fish. The interesting question remains as to how both the a and y chains independently lost one of the four Ch domains present in the human fx chain. 

Compression tends to increase background noise, especially during periods of silence. The Attack and Release controls can help eliminate this, but many times the only solution is to use a Noise Gate plug-in just after the Compression plug-in in the FX chain. 

Some FX are better used at tbe track level and some are better used in the Mixer window, but all ophons are possible for maximum flexibility. Specific recommendations are given after a brief discussion of FX chains in the next section and in the descriptions of the actual plug-ins. 

The substituted Bfx and Fx exhibit the isomerization or, well known, ring-chain tautomerism equihbrium depicted in Scheme 3. This phenomenon... 

Scheme 3 Bfxs and Fxs ring-chain tautomerism and its implications...

For initiated oxidation, the inhibitory criterion could be defined as the ratio v0/v or (v0/ v — v/v0), where v0 and v are the rates of initiated oxidation in the absence and presence of the fixed concentration of an inhibitor, respectively. Another criterion could be defined as the ratio of the inhibition coefficient of the combined action of a few antioxidants / to the sum of the inhibition coefficients of individual antioxidants when the conditions of oxidation are fixed (fx = IfiXi where f, and x, are the inhibition coefficient and molar fraction of z th antioxidant terminating the chain). It should, however, be noted that synergism during initiated oxidation seldom takes place and is typical of autoxidation, where the main source of radicals is formed hydroperoxide. It is virtually impossible to measure the initial rate in the presence of inhibitors in such experiments. Hence, inhibitory effects of individual inhibitors and their mixtures are usually evaluated from the duration of retardation (induction period), which equals the span of time elapsed from the onset of experiment to the moment of consumption of a certain amount of oxygen or attainment of a certain, well-measurable rate of oxidation. Then three aforementioned cases of autoxidation response to inhibitors can be described by the following inequalities (r is the induction period of a mixture of antioxidants). 

Our initial, small models of an isolated cellulose chain ranged from the dimer (cellobiose) to the octamer. The dynamics of these fragments have thus far been simulated only in vacuum, using different potential energy functions such as those of MM2(85) (9) and AMBER (10), with and without contributions from electrostatic terms and hydrogen bonds, etc. (The program DISCOVER, customized for carbohydrates and for operation on the Alliant FX/80 computer, has been used (12).) Generally, the time span for the simulations has been of the order of several hundred picoseconds to 1 nanosecond. 

For a single chain of n segments confined in the adsorbed polymer layer with thickness D, the chemical potential fx is given by... 

In the semidilute region, the repulsion between adsorbed chains is dominated by the osmotic term. Hence, the chemical potential fx is represented by... 

The time scale of different steps of electron transfer along the PS I cascade system is also similar to those ofthe electron jump in bacterial RCs. The primary transfer from the excited chlorophyll dimer, primary donor P, to A0 takes place with a time constant of about 25 ps. The next step from A0 to a secondary acceptor occurs in 200-600 ps. The recombination time constants ofP+ with reduced intermediate acceptors increase as the electron moves along the chain, and range from nanoseconds for transition A0 — P+ to millscconds for transition reduce FX to P+ (Shuvalov and Krasnovsky, 1981 Schloder et al., 1998 Shmidt et al., 2000 Shmidt et al., Guergova-Kuras et. al., 2001 Setif et al., 2001 Vassiliev et all., 2001 Gobets et al., 2001 and references therein). Kinetic and spectral inhomogenity of samples of PS I has been reported (Shmidt et al., 2000 ... 

The long chain ammonium salt and amine surfactants showed better selectivity and calculated MON s. The improvement in MON ranged from about 0.4 at an OSV of 0.08 V/Hr/V to more than 2 at 0.7 V/Hr/V. The space velocity was normally 0.077 and was cycled during the course of a run between this value and higher rates which were held until the product quality was steady. A comparison of selectivity to Cg s in the C fraction is shown in Figure 16. Octylamine was intermediate in its ability to improve selectivity while two of the surfactants which were anionic (FC-95 and FX-161), showed no improvement under well mixed conditions. In addition the tetramethylammonlum ion which is not surface active was also an ineffective additive. 

Spectroscopic and crystallographic studies have identified four Fe S clusters in the membrane-bound photosynthetic electron transport chain of plant and cyanobacterial chloro-plasts. One is the Rieske-type [2Fe-2S] + + center in the cyt b(,f complex, which catalyzes electron transfer from plasto-quinol to plastocyanin with concomitant proton translocation, and is functionally analogous to the cyt bc complex, with cyt / in place of cyt The remainder are low-potential [4Fe 4S] + + centers in Photosystem I which constitute the terminal part of the electron transfer chain that is initiated by the primary donor chlorophyll. One is a very low-potential [4Fe S] + + center, Fx (Em =-705 mV), that bridges two similar subunits (PsaA and PsaB) and is coordinated by two cysteines from each subunit in a C-Xg-C arrangement. This cluster transfers electrons to the 2Fe-Fd acceptor via an electron transfer chain composed of Fa, a [4Fe S] + + cluster with Em = -530 mV, and Fb, a [4Fe S] + + clusters with Em = -580 mV. Fa and Fb are in a low-molecular weight subunit (PsaC, 9 kDa) that shows strong sequence and structural homology with bacterial 8Fe-Fds. The center-to-center distance between Fx and Fa and between Fa and Fb are 14.9 A and 12.3 A, respectively, well... 

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