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Coils panel

Polycold (vacuum technology) A term sometimes used for a cryocondensation (Meissner) coil/panel in the process chamber. Polycold is the company that popularized such traps in the US. [Pg.676]

Costs of the cements (in 1960) varied from 37 to 63 cents per pound, with requirements running from about 0.27 Ib/ft of %-in out-side-diameter tubing to 1.48 Ib/ft of 1-in pipe. Panel coils require to 1 Ib/ft". A rule of thumb for preliminaiy estimating is that the per-foot installed cost of tracer with cement is about double that of the tracer alone. [Pg.1052]

Panel Coils Immersed in Liquid Overall Average Heat-Transfer Coefficients ... [Pg.1056]

Panel coils 50 lh./sq. in. gage steam Boiling water 212 29 48-54... [Pg.1057]

Data courtesy of Thermon Manufacturing Co. f External surface of tubing or side of panel coil facing tank. [Pg.1057]

The heat and flame resistance coupled with good electrical insulation characteristics, which includes in some grades good arcing and arc tracking resistance, has led to PPS replacing some of the older thermosets in electrical parts. These include connectors, coil formers, bobbins, terminal blocks, relay components, moulded bulb sockets for electric power station control panels, brush holders, motor housings, thermostat parts and switch components. [Pg.595]

For MTHW and HTFIW systems, heat emitters may be as for LTFIW systems, except that, for safety reasons, units with accessible surfaces at water temperature would not normally be employed. Embedded panel coils may be used in conjunction with a MTHW or HTHW distribution system, with insulating sleeves around the coil piping to reduce the heat flow. Alternatively, the coils can be operated as reduced temperature secondary systems by allowing only a small, carefully controlled proportion of flow temperature water to be mixed with the water circulating in the coils. [Pg.408]

Copper pipes For plumbing above ground, copper is supplied in both half-hard and hard conditions. It has sufficient strength to require only few supports, and can be bent cold, in the small sizes, either by hand or with a portable bending machine. Copper is also supplied in the fully soft condition in coils for laying underground, for heating-panels, etc. [Pg.57]

In addition to the above subcategories, porcelain enameling on continuous strip is a subdivision within this industry. However, because there are only two plants in the U.S. producing this product, a separate subcategory is not necessary. These plants start with coils of steel, aluminum, or aluminized steel, porcelain enamel them and either recoil them for sale to metal fabricators or shear them into pieces for use as architectural panels or chalkboards. The estimated production was 2.0 x 106 m2 (22 x 106 ft2). This figure represents the area of enamel applied. For multiple coats, the area for each coat is considered. [Pg.310]

Fig. 2. Ball-and-stick representations of two differently oriented asparagine ladders of (A) W-arcade taken from the crystal structures of pectate lyase C (Lietzke et al., 1996) and (b) ppl-arcade taken from l DP-.V-aretylglucosamine acyltransferase (Raetz and Roderick, 1995). b, l, and so on refer to a one-letter conformational code (Fig. IOC). The ladders are viewed from within the respective /(-solenoids. The arrow shows the orientation (N- to C-terminal) of the solenoid. Oxygen atoms are in red, nitrogen in blue, and carbon in green. Dotted lines designate H-bonds of side chains (red) and inter-coil H-bonds of the polypeptide backbone (black). Except for the ladder-forming asparagines, only the backbones of the coils are shown. Panels are reprinted from Hennetin et al. (2006) with the permission of the publisher. Fig. 2. Ball-and-stick representations of two differently oriented asparagine ladders of (A) W-arcade taken from the crystal structures of pectate lyase C (Lietzke et al., 1996) and (b) ppl-arcade taken from l DP-.V-aretylglucosamine acyltransferase (Raetz and Roderick, 1995). b, l, and so on refer to a one-letter conformational code (Fig. IOC). The ladders are viewed from within the respective /(-solenoids. The arrow shows the orientation (N- to C-terminal) of the solenoid. Oxygen atoms are in red, nitrogen in blue, and carbon in green. Dotted lines designate H-bonds of side chains (red) and inter-coil H-bonds of the polypeptide backbone (black). Except for the ladder-forming asparagines, only the backbones of the coils are shown. Panels are reprinted from Hennetin et al. (2006) with the permission of the publisher.
B) Surface and stick representation of the model, viewed down the fibril axis. (The top coil is shown as sticks, with the remainder showing van derWaals radii.) The glutamine side chains are proposed to form hydrogen-bonded stacks parallel to the fibril axis. The large diameter of the cylinder results in a pore down the center. Both panels were generated with Pymol (DeLano, 2002). [Pg.258]

India s Reva EV can travel at about 35 mph. The power system is eight 6-volt EV type lead add batteries. The dent-proof body panels are made of high impad ABS (acrylonitrile butadiene styrene). It has side impact beams and electronic regenerative braking. The suspension is McPherson struts in front and coil springs in the rear. It is a two-door hatchback that... [Pg.259]

Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation. Fig. 2. NAPI facilitates H2A, H2B release from nucleosomes that are on positively coiled DNA (A) but not negatively coiled DNA (B). The positively coiled DNA (6.0 kb) with a superhelical density of + 0.05 and negatively coiled DNA (6.0 kb) with a superhelical density of -0.05 were reconstituted with lysine, arginine-labeled histones H3, H4, H2A, H2B by NaCl dialysis from 2.0 M to 1.2 M to 0.6 M to 0.1 M NaCl over a 14 h period. The samples were incubated with NAPI at 35 °C for 5 min and applied to a 5-20% sucrose/100 mM NaCl/40 mM Tris, pH 7.8 gradient. After sedimentation at 200,000 X g for 5 h, fractions were collected and the distribution of DNA (bottom panel) was determined on agarose gel and the distribution of protein (top panel) on SDS-PAGE followed by fluorography. These data are unpublished observations (V. Levchenko and V. Jackson). The deg-H2A is degraded H2A in which a 15 amino acid peptide of the C terminal has been proteolytically removed. When H2A, H2B is no longer present in a nucleosome, the C terminal region is sensitive to proteolysis [126] from a protease which is a minor contaminate in the NAPI preparation.
Fig. 6. Deconvolved amide F region FTIR spectra of apo- and heme-hemopexin. The amide F FTIR spectra of apo- and heme-hemopexin in D2 O were recorded and curve-fitted to resolve the individual bands. The differences between the original and fitted curves are shown in the upper traces in the panels. The estimated helix (15%), beta (54%), turn (19%), and coil (12%) content of the apo-protein are not significantly changed upon heme binding 104). This analysis was required because of the positive 231-nm elhpticity band in hemopexin and is consistent with the derived crystal structure results. Fig. 6. Deconvolved amide F region FTIR spectra of apo- and heme-hemopexin. The amide F FTIR spectra of apo- and heme-hemopexin in D2 O were recorded and curve-fitted to resolve the individual bands. The differences between the original and fitted curves are shown in the upper traces in the panels. The estimated helix (15%), beta (54%), turn (19%), and coil (12%) content of the apo-protein are not significantly changed upon heme binding 104). This analysis was required because of the positive 231-nm elhpticity band in hemopexin and is consistent with the derived crystal structure results.
Automated Hydrometers. One form of hydrometer utilizes an opaque stem which, as the stem rises and falls, effects the amount of light which passes through a slit to a photocell. In this way. the photocell output is proportional to specific gravity and may be recorded by an electric instrument. In another industrial version, designed for remote transmission, the hydrometer is contained within a metal cylinder. A rod connects the bottom portion of the float to an armature, which moves vertically between inductance coils. Changesin inductance are transmitted by cable to a central instrument panel receiving instrument. [Pg.1529]

Fig. 3. Conformation of the switch-2 cluster and neck linker/neck region in various members of the kinesin superfamily. The upper four panels (A, B, E, F) show crystal structures of N-type kinesins with their motor domain at the N-terminus and the neck at the C-terminus. (C), (D), (G), and (H) show C- and M-type kinesins with their neck N-terminal to the motor domain, except for PoKCBP (G) where the C-terminal neck mimic is shown instead of the N-terminal neck (which is not included in the crystal structure). Each structure is shown in two orientations that differ by a rotation of 90 degrees. Rat conventional kinesin (RnKHC [A]) has been chosen to define standard orientations with the neck helix a7 parallel/perpendicular to the drawing area. Orientations for the other structures have been determined by least-squares superposition of their P-loop regions with that of RnKHC (using 11 Ca-atoms of residues F83-T93 in RnKHC). (B), (C), and (D) show the structures of dimeric constructs with the second motor domain in pale colors. The Ned structure in (C) is 180-degree symmetric the symmetry axis is oblique to the drawing plane and coincides with the axis of the coiled-coil that is formed by the two neck helices. In the asymmetric structure of the Ned N600K mutant (D), the second motor domain (pale) is rotated by about 75 degrees around an axis perpendicular to the coiled-coil. The structures shown in (A), (B), (F), and (G) have their switch-2 cluster in permissive conformation, whereas the conformation of structures (C), (D), (E), and (H) is obstructive, as can be told by observing the slope of the extended switch-2 helix a4. Color code red, switch-2 cluster including the extended... Fig. 3. Conformation of the switch-2 cluster and neck linker/neck region in various members of the kinesin superfamily. The upper four panels (A, B, E, F) show crystal structures of N-type kinesins with their motor domain at the N-terminus and the neck at the C-terminus. (C), (D), (G), and (H) show C- and M-type kinesins with their neck N-terminal to the motor domain, except for PoKCBP (G) where the C-terminal neck mimic is shown instead of the N-terminal neck (which is not included in the crystal structure). Each structure is shown in two orientations that differ by a rotation of 90 degrees. Rat conventional kinesin (RnKHC [A]) has been chosen to define standard orientations with the neck helix a7 parallel/perpendicular to the drawing area. Orientations for the other structures have been determined by least-squares superposition of their P-loop regions with that of RnKHC (using 11 Ca-atoms of residues F83-T93 in RnKHC). (B), (C), and (D) show the structures of dimeric constructs with the second motor domain in pale colors. The Ned structure in (C) is 180-degree symmetric the symmetry axis is oblique to the drawing plane and coincides with the axis of the coiled-coil that is formed by the two neck helices. In the asymmetric structure of the Ned N600K mutant (D), the second motor domain (pale) is rotated by about 75 degrees around an axis perpendicular to the coiled-coil. The structures shown in (A), (B), (F), and (G) have their switch-2 cluster in permissive conformation, whereas the conformation of structures (C), (D), (E), and (H) is obstructive, as can be told by observing the slope of the extended switch-2 helix a4. Color code red, switch-2 cluster including the extended...
After the assignment process is complete, various types of NMR data can be used to build up a picture of the secondary structure of the peptide (based on coupling constants, chemical shifts, and NOEs) and then, if required, a full 3D structure can be determined. Figure 6 shows some of this information for Vcl.l. As noted earlier, deviations from random coil chemical shifts provide an indication of secondary structure, and in the case of Vcl.l. a region of negative aH secondary shifts provides a first indication that the helix typically present in a-conotoxins is indeed present in Vcl.l (Fig. 6A). This conclusion is supported by the CSI, coupling, and NOE data in Fig. 6B. Finally, the 3D structure is shown in various representations in the lower panels of the figure (58). [Pg.97]

Fig. 1.3. Paramagnetic relaxation enhancement profiles for apomyoglobin unfolded at pH 2.3 in the presence (left panels) and absence (right panels) of 8M urea. Data for spin labels attached at residues 18 and 77 is shown. The plots show the ratio of HSQC cross-peak intensity with the spin label oxidized (paramagnetic) and reduced (diamagnetic) as a function of residue number. The solid lines in the left panels represent the broadening profile expected for a random coil polypeptide. The figure is adapted from data reported in [14]. The positions of the helices in holomyoglobin are shown by the bars at the top of the figure... Fig. 1.3. Paramagnetic relaxation enhancement profiles for apomyoglobin unfolded at pH 2.3 in the presence (left panels) and absence (right panels) of 8M urea. Data for spin labels attached at residues 18 and 77 is shown. The plots show the ratio of HSQC cross-peak intensity with the spin label oxidized (paramagnetic) and reduced (diamagnetic) as a function of residue number. The solid lines in the left panels represent the broadening profile expected for a random coil polypeptide. The figure is adapted from data reported in [14]. The positions of the helices in holomyoglobin are shown by the bars at the top of the figure...

See other pages where Coils panel is mentioned: [Pg.1051]    [Pg.874]    [Pg.1218]    [Pg.1219]    [Pg.1055]    [Pg.22]    [Pg.117]    [Pg.122]    [Pg.1051]    [Pg.874]    [Pg.1218]    [Pg.1219]    [Pg.1055]    [Pg.22]    [Pg.117]    [Pg.122]    [Pg.279]    [Pg.389]    [Pg.251]    [Pg.1540]    [Pg.20]    [Pg.23]    [Pg.327]    [Pg.327]    [Pg.410]    [Pg.361]    [Pg.352]    [Pg.21]    [Pg.50]    [Pg.57]    [Pg.244]    [Pg.120]    [Pg.251]    [Pg.14]    [Pg.220]    [Pg.12]    [Pg.132]    [Pg.28]    [Pg.60]   
See also in sourсe #XX -- [ Pg.11 , Pg.12 , Pg.13 , Pg.14 , Pg.15 , Pg.16 , Pg.17 , Pg.18 , Pg.19 , Pg.20 ]




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