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Data transfer binding

Data Transfer Binding Data transfer binding determines for every data movement operation which bus to use. Two factors might affect the number of switches needed to connect both the register files and the function units to and from the buses. [Pg.295]

Cost Function for Data Transfer Binding The cost, of assigning a... [Pg.297]

A set of data transfers will be grouped into a class if they take place simultaneously. The classes are sorted according to their sizes. The data transfer binding algorithm is also a branch-and-bound search with a cost function for predicting buses utilization. [Pg.298]

The mechanism that is consistent with biochemical, enzymological and structural data involves binding of arginine, in which the side-chain of Glu277 plays an important role, attack of the nucleophilic metal-bridged hydroxyl ion, formation of a neutral, tetrahedral intermediate which is stabilized by the dinuclear Mn(II) centre, and finally proton transfer from Hisl41, followed by release of the two products (Figure 16.5). [Pg.274]

The processor synthesizer, which will be presented in the remaining of this chapter, consists of scheduling, data path binding and controller synthesis. Its output is a set of connected Register Transfer Level (RTL) modules which may be... [Pg.283]

After operation assignment and register file allocation, the number of additional switches needed for each data-transfer-to-bus binding becomes clear. [Pg.295]

The data path binding problem is divided into two phases data path construction and data path refinement. A branch-and-bound search algorithm is used to construct the initial data path based on a set of observations. During the data path refinement phase, we rip up a mixture of variables, data transfers and operations and relocate them. The refinement is augmented with a randomized selection process to prevent itself from being trapped in a local optimal. [Pg.305]

Data from a single study in dogs suggest that hepatic first-pass metabolism may limit systemic availability of the parent compound following oral exposure (Braeckman et al. 1983). Placental transfer of methyl parathion was demonstrated in pregnant rats 1-3 days before parturition. Thirty minutes after administration, both methyl parathion and methyl paraoxon were found in fetal brain, liver, and muscle methyl parathion, but not methyl paraoxon, was detected in placenta and maternal liver (Ackermann and Engst 1970). Methyl parathion binds reversibly to serum albumin, but is readily distributed to the tissues (Braeckman et al. 1980, 1983). [Pg.100]

Figure 18.4 Structures of heme/Cu oxidases at different levels of detail, (a) Position of the redox-active cofactors relative to the membrane of CcO (left, only two obligatory subunits are shown) and quinol oxidase (right), (b) Electron transfer paths in mammalian CcO. Note that the imidazoles that ligate six-coordinate heme a and the five-coordinate heme are linked by a single amino acid, which can serve as a wire for electron transfer from ferroheme a to ferriheme as. (c) The O2 reduction site of mammalian CcO the numbering of the residues corresponds to that in the crystal structure of bovine heart CcO. The subscript 3 in heme as and heme 03 signifies the heme that binds O2. The structures were generated using coordinates deposited in the Protein Data Bank, lari [Ostermeier et al., 1997] Ifft [Abramson et al., 2000] (a) and locc [Tsukihara et al., 1996] (b, c). Figure 18.4 Structures of heme/Cu oxidases at different levels of detail, (a) Position of the redox-active cofactors relative to the membrane of CcO (left, only two obligatory subunits are shown) and quinol oxidase (right), (b) Electron transfer paths in mammalian CcO. Note that the imidazoles that ligate six-coordinate heme a and the five-coordinate heme are linked by a single amino acid, which can serve as a wire for electron transfer from ferroheme a to ferriheme as. (c) The O2 reduction site of mammalian CcO the numbering of the residues corresponds to that in the crystal structure of bovine heart CcO. The subscript 3 in heme as and heme 03 signifies the heme that binds O2. The structures were generated using coordinates deposited in the Protein Data Bank, lari [Ostermeier et al., 1997] Ifft [Abramson et al., 2000] (a) and locc [Tsukihara et al., 1996] (b, c).
Electrochemical reactions are driven by the potential difference at the solid liquid interface, which is established by the electrochemical double layer composed, in a simple case, of water and two types of counter ions. Thus, provided the electrochemical interface is preserved upon emersion and transfer, one always has to deal with a complex coadsorption experiment. In contrast to the solid/vacuum interface, where for instance metal adsorption can be studied by evaporating a metal onto the surface, electrochemical metal deposition is always a coadsorption of metal ions, counter ions, and probably water dipols, which together cause the potential difference at the surface. This complex situation has to be taken into account when interpreting XPS data of emersed electrode surfaces in terms of chemical shifts or binding energies. [Pg.78]

There is a body of data in the literature which indicates that dissolved humic materials may play a significant and previously overlooked role in the behavior of organic water pollutants. It has been shown that dissolved humic materials can affect degradation rates and phase transfer rates for a number of compounds. A number of methods have been developed in this research and by other researchers which can make quantitative measurements of the extent of binding between organic water pollutants and dissolved humic materials. Hopefully these methods will be used by other researchers to gain more insight into this phenomenon. [Pg.227]


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See also in sourсe #XX -- [ Pg.285 , Pg.294 , Pg.295 ]




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