Sectional plates

After each series of experiments with beams of various intensity the section plate would be removed from the cell and disassembled, with radioactive silver washed out by nitric acid. Radioactivity of the solutions obtained was measured by a multichannel spectrometric scintillation y-counter with sensitivity of up to 10 G, i. e. around 10 of atoms which, according to calculations, is 10 times lower than sensitivity of ZnO sensor 10 G or 10 of Ag atoms respectively [28]. This difference in sensitivity lead to great inconveniences when exposing of targets was used in above methods. Only a few seconds were sufficient to expose the sensor compared to several hours of exposure of the scintillation counter in order to let it accumulate the overall radioactivity. It is quite evident that due to insufficient stability during a long period of exposure time an error piled up. 

Diagrams and photographs, of sectional plates, are given in Volume 2, Chapter 11. 

The plates are not fixed to the vessel wall, as they are with sectional plates, so there is no positive liquid seal at the edge of the plate, and a small amount of leakage will occur. In some designs the plate edges are turned up round the circumference to make better contact at the wall. This can make it difficult to remove the plates for cleaning and maintenance, without damage. 

The width of the support ring for sectional plates will normally be 50 to 75 mm the support ring should not extend into the downcomer area. A strip of unperforated plate will be left round the edge of cartridge-type trays to stiffen the plate. 

These recent tests were conducted at applied stress levels similar to those that might be experienced by ASME Section Vm, Division 2 vessels. Test exposure times exceeded 50,000 hours depending on applied stress and temperature. The test specimens were from weldments of thick section plates and represented base metal, weld metal, and heat-affected zone. Detrimental effects of hydrogen were found down to the Figure 1 limit of 850°F (454°C) at 2000 pounds per square inch absolute (14 megapascals) and 3000 pounds per square inch absolute (21 megapascals) hydrogen partial pressure. 

On a volume basis, contaminated rinsewater accounts for the majority of plating process waste. As shown in the previous sections, plating processes can involve many rinsing steps. Rinsewater is used to wash off the drag-out from a workpiece after it is removed from a bath. Drag-out refers to the excess solution that adheres to the workpiece surface and gets... 

Fig. 2. Acetyl-CoA carboxylase. (A) Eukaryotic ACCs contain -2300 residues organized into three functional domains — biotin carboxylase (BC), biotin carboxyl carrier protein (BCCP), and carboxyltransferase (CT). The role of the region between the biotin carboxyl carrier and carboxyltransferase domains is unknown. The biotin carboxyl carrier protein contains a typical conserved biotin attachment-site motif, VMKMV. The sites of phosphorylation are indicated by asterisks. (B) Electron micrograph of polymerized rat acetyl-CoA carboxylase (F. Ahmad, 1978). (C) Crystal structure of the biotin carboxylase domain of the yeast enzyme. In the presence of soraphen A, the biotin carboxyl carrier protein domain forms an inactive monomer the likely position of the modeled ATP-binding site is shown (adapted from Ref. [2]). (D) Crystal structure of the dimeric carboxyltransferase domain of the yeast enzyme. Although acetyl-CoA was included in the crystallization, density was observed only for CoA at one site and adenine at the other (adapted from Ref. [2]). (E) NMR structure of the biotin carboxyl carrier apoprotein domain of the human ACC2 The lysine attachment site for biotin is shown (RIKEN Structural Genomics/Proteomics Initiative, 2006). (See color plate section, plate no. 3.)...

Fig. 5. Architecture of the fungal FAS. (A) Structural overview of the barrel-shaped molecule showing the location of the equatorial wheel composed of the six alpha subunits flanked by two domes, each composed of a p subunit trimer. The barrel is 270 A long and 230 A wide at the equator. (B) Location of the structural underpinnings of the molecule with the catalytic domains removed. (C) Organization of the alpha-subunit hexamer. (D) Organization of one p-subunit trimer (adapted from Lomakin et al. [13] with permission). (See color plate section, plate no. 4.)...

Fig. 6. Structure of the animal FAS. (A) An overview of the entire complex (reproduced with permission of Maier et al. [9]). Fitted homologous domains are shown with a semi-transparent surface representation of the experimental 4.5-A-resolution electron density. Two white stars indicate the pseudosymmetry-related suggested attachment regions for the ACP and thioesterase ACP and TE, where more density is visible on the right side. MAT, malonyl/acetyltransferase. (B) High-resolution structures of the ACP and MAT domains (Structural Genomics Consortium) and the TE domain (F.A. Quiocho, 2004) of the human FAS showing locations of active-site residues. The gray region of the MAT (residues 422-484) represents a structured linker region that probably interacts with the adjacent KS domain and is not part of the MAT catalytic domain. (See color plate section, plate no. 5.)...

Fig. 6. Coordinated transcriptional regulation of fatty acid desaturases and elongases in mammals. PUFA, polyunsaturated fatty acids +, stimulation inhibition LXR, liver X receptor RXR retinoid X receptor SREBP, sterol regulatory element binding protein ChREBP, carbohydrate response element binding protein Mix, Max-like receptor PPAR-ot, peroxisome proliferator activated receptor alpha LXRE, liver X receptor response element SRE, sterol response element ChoRE, carbohydrate response element PPRE, peroxisome proliferator response element. (See color plate section, plate no. 6.)...

Fig. 6. Translocation of CTP phosphocholine cytidylyltransferase (CT) from an inactive soluble form (CTsol) to a membrane-associated activated form (CTm). The reversible interaction of CT with membranes involves the amphipathic helical region lying on the surface of the membrane so that the hydrophilic region interacts with the negatively charged lipid head groups and the hydrophobic side intercalates into the membrane core. N, amino terminal domain C, carboxyl terminal domain M, membrane-binding domain. Figure kindly supplied by Prof. R. Cornell, Simon Fraser University. (See color plate section, plate no. 7.)...

Fig. 4. Crystal structure of the outer membrane phospholipase A dimer from E. coli shown in the plane of the membrane. The top half of the molecule is located in the lipopolysaccharide monolayer facing the exterior of the cell. The phospholipid monolayer of the outer cell membrane would be located around the bottom half of the protein. Two calcium ions are shown at the active sites while Ser-144 of each active site is covalently modified with a hexadecylsulfonyl moiety represented in a ball and stick format. Structure is adapted from Ref. [12]. (See color plate section, plate no. 8.)...

Fig. 9. Crystal structure of group IV cytosolic PLAj showing the C2 and catalytic domain. The two calcium ions bound to the C2 domain and the active-site Ser-228 are highlighted. The phospholipid interface would be parallel to the top surface of the molecule as shown. A flexible region between residues 499 and 538 is not seen in the crystal structure but contains Ser-505, the approximate position of which is indicated by the arrow. The N-and C-termini of the protein are indicated. Adapted from A. Dessen (1999) and Ref. [24]. (See color plate section, plate no. 9.)...

Fig. 11. Crystal structure of the PLD from Streptomyces sp. showing two active-site histidines in space-filling format together with the N- and C-termini of the protein. Adapted from I. Leiros (2000). (See color plate section, plate no. 11.)...

Fig. 5. Ribbon diagram of the structure of ovine PGH synthase-1 homodimer intendigitated via its membrane-binding domain (MBD) into the lumenal surface of the endoplasmic reticulum. (See color plate section, plate no. 12.)...

Fig. 4. The lipid pocket of apo B. Apo B22.5 is represented with P-strands shown as green arrows and a-helices shown as turquoise tubes. l-Palmitoyl-2-oleoylphosphatidyIcholine (POPC) is shown with carbon atoms in gray and oxygens in red. There are 34 POPC molecules in the large opening and 14 POPC molecules in the small opening. Thus, a total of 48 POPC molecules fit into the lipid pocket. From Ref. [24], with permission. (See color plate section, plate no. 16.)...

Fig. 1. Summary of major forward and reverse lipid transport pathways through the extracellular compartment that link the liver and intestine with peripheral tissues. FC, unesterified cholesterol. For other abbreviations see list of abbreviations. (See color plate section, plate no. 17.)...

Similar to the above section, plate bearing tests or pressuremeter tests carried out in boreholes are applicable for the assessment of bearing capacity and settlement. For initial reference to assess engineering properties of engineered fill, empirical chart and table in NAVFAC (1971) manual publication reproduced in Figure 3.12 and Table 3.9 may be of assistance. 

The stiffener and the effective width of box-section plate were considered a column or longitudinal strut supported between transverse T-stiffeners. The stiffened sections resulted in slenderness ratios (KLIr) of less than 115. The compressive resistance of the effective stiffener and plate section was compared to the computed axial stress due to the combined effects of bending md cixicil load. 

In days of old, distillation was the most powerful means for separating volatile compounds. A distillation column was divided into sections plates) in which liquid and vapor equilibrated with each other. The more plates on a column, the more equilibration steps and the better the separation between compounds with different boiling points. 

More specifically, let the plates be numbered from the top to the bottom of a section. Plate number 1 is constituted by the condenser. The boundary of... 

Now, lV)j = W fi for the enriching section plates above the side product withdrawal plate, whereas is valid for plates below it. Therefore... 

---