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Part ribbon

Conventional feeder screws have full-face flights welded to a centre shaft or tube. Uniform pitch screws are sometimes used in simple feeding applications. In order to secure differential intake of product along the axis of a screw, a range of techniques can be adopted, either individually or in combination where appropriate. Typical constructional features are (see Fig. 4.5) stepped pitch variable pitch stepped or taper centre tube or shaft variable screw diameter part ribbon or shaftless construction. (Occasionally the construction is stepped on the outside diameter.)... [Pg.70]

Moving-belt (ribbon or wire) interface. An interface that continuously applies all, or a part of, the effluent from a liquid chromatograph to a belt (ribbon or wire) that passes through two or more orifices, with differential pumping into the mass spectrometer s vacuum system. Heat is applied to remove the solvent and to evaporate the solute into the ion source. [Pg.433]

Figure 2.14 shows examples of both cases, an isolated ribbon and a p sheet. The isolated ribbon is illustrated by the structure of bovine trypsin inhibitor (Figure 2.14a), a small, very stable polypeptide of 58 amino acids that inhibits the activity of the digestive protease trypsin. The structure has been determined to 1.0 A resolution in the laboratory of Robert Huber in Munich, Germany, and the folding pathway of this protein is discussed in Chapter 6. Hairpin motifs as parts of a p sheet are exemplified by the structure of a snake venom, erabutoxin (Figure 2.14b), which binds to and inhibits... [Pg.26]

Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)... Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)...
Figure 14.2 Models of a collagen-like peptide with a mutation Gly to Ala in the middle of the peptide (orange). Each polypeptide chain is folded into a polyproline type II helix and three chains form a superhelix similar to part of the collagen molecule. The alanine side chain is accommodated inside the superhelix causing a slight change in the twist of the individual chains, (a) Space-filling model, (b) Ribbon diagram. Compare with Figure 14.1c for the change caused by the alanine substitution. (Adapted from J. Bella et al.. Science 266 75-81, 1994.)... Figure 14.2 Models of a collagen-like peptide with a mutation Gly to Ala in the middle of the peptide (orange). Each polypeptide chain is folded into a polyproline type II helix and three chains form a superhelix similar to part of the collagen molecule. The alanine side chain is accommodated inside the superhelix causing a slight change in the twist of the individual chains, (a) Space-filling model, (b) Ribbon diagram. Compare with Figure 14.1c for the change caused by the alanine substitution. (Adapted from J. Bella et al.. Science 266 75-81, 1994.)...
Figure 26.9 X-ray crystal structure of citrate synthase. Part (a) is a space-filling model and part (b) is a ribbon model, which emphasizes the a-helical segments of the protein chain and indicates that the enzyme is dimeric that is, it consists of two identical chains held together by hydrogen bonds and other intermolecular attractions. Part (cl is a close-up of the active site in which oxaloacetate and an unreactive acetyl CoA mimic are bound. Figure 26.9 X-ray crystal structure of citrate synthase. Part (a) is a space-filling model and part (b) is a ribbon model, which emphasizes the a-helical segments of the protein chain and indicates that the enzyme is dimeric that is, it consists of two identical chains held together by hydrogen bonds and other intermolecular attractions. Part (cl is a close-up of the active site in which oxaloacetate and an unreactive acetyl CoA mimic are bound.
Phthalate esters are widespread contaminants and the dialkyl phthalates are hydrolyzed before degradation of the resulting phthalate (Eaton and Ribbons 1982), which is discussed in Chapter 8, Part 3. For dimethyl phthalate, dimethyl terephthalate, and dimethyl isophthalate only partial hydrolysis may take place (Li et al. 2005). Cocaine is hydrolyzed to benzoate and ecgonine methyl ester by a strain of Pseudomonas maltophilia (Britt et al. 1992). [Pg.569]

FIGURE 5-11 Ribbon diagram of an NBD dimer (PDB 160). 3 strands are depicted as arrows and a helices as coiled ribbons. The two nucleotides, shown as stick models, bind to form part of the interface that stabilizes the dimeric interaction. (With permission from Fig. 5 of reference [88].)... [Pg.83]

Two maintenance workers were replacing part of a ribbon in a large ribbon mixer. The main switch was left energized the mixer was stopped with one of three start-stop buttons. [Pg.552]

Figure 4.16 The structure of yeast tRNAplle (a) the cloverleaf form of the base sequence tertiary base-pairing interactions are represented by thin red lines connecting the participating bases. Bases that are conserved in all tRNAs are circled by solid and dashed lines, respectively. The different parts of the structure are colour-coded, (b) The X-ray structure showing how the different base-paired stems are arranged to form an L-shaped molecule. The sugar-phosphate backbone is represented as a ribbon with the same colour scheme as in (a). (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.)... Figure 4.16 The structure of yeast tRNAplle (a) the cloverleaf form of the base sequence tertiary base-pairing interactions are represented by thin red lines connecting the participating bases. Bases that are conserved in all tRNAs are circled by solid and dashed lines, respectively. The different parts of the structure are colour-coded, (b) The X-ray structure showing how the different base-paired stems are arranged to form an L-shaped molecule. The sugar-phosphate backbone is represented as a ribbon with the same colour scheme as in (a). (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.)...
In many fracture tests, a splitting method was employed. Figures 8 to 10 schematically indicate three of the arrangements used. In Fig. 8, a slice, h cm thick, is separated from the rest of the solid by pushing in a wedge which may be as thin as 0.01 cm but may also be more robust and have one of various shapes also the part broken off may be as thick as the remainder. In Fig. 9, a plate, 2h cm thick and w cm wide, is split in the middle to the depth c cm, and the force /required to extend the fissure is measured. Figure 10 shows peeling a ribbon, h cm thick, is peeled off the main body of an identical solid. [Pg.34]

Fig. 2.8 Cleavage in the amphiboles. (A) Schematic representation of the characteristic stacked amphibole I-beams in the three-dimensional structure. A tetrahedral portion of an I-beam is labeled "silica ribbon." The octahedral portion is labeled "cation layer" and represented by solid circles. One of the possible cleavage directions (110) along planes of structural weakness is indicated by the line A-A stepped around the I-beams in the lower part of the diagram. (B) Cross section of the stacked I-beams with the directions of easy cleavage indicated. There is a lower density of bonds between I-beams in the crystallographic directions (110) and (110). These directions, parallel to the c axis and the length of the chains, are the planes of cleavage. The minimum thickness of a rhombic fragment produced through cleavage is 0.84 nm. Fig. 2.8 Cleavage in the amphiboles. (A) Schematic representation of the characteristic stacked amphibole I-beams in the three-dimensional structure. A tetrahedral portion of an I-beam is labeled "silica ribbon." The octahedral portion is labeled "cation layer" and represented by solid circles. One of the possible cleavage directions (110) along planes of structural weakness is indicated by the line A-A stepped around the I-beams in the lower part of the diagram. (B) Cross section of the stacked I-beams with the directions of easy cleavage indicated. There is a lower density of bonds between I-beams in the crystallographic directions (110) and (110). These directions, parallel to the c axis and the length of the chains, are the planes of cleavage. The minimum thickness of a rhombic fragment produced through cleavage is 0.84 nm.
Figure 4.2 This three-dimensional image of a protein shows the many twists and folds in its structure. The coils, called alpha helices, and the ribbons, called beta pleated sheets, are generally determined by the amino acid sequence of the protein and how the amino acids in different parts form weak bonds with each other. The shape of a protein is often critical for its function. Figure 4.2 This three-dimensional image of a protein shows the many twists and folds in its structure. The coils, called alpha helices, and the ribbons, called beta pleated sheets, are generally determined by the amino acid sequence of the protein and how the amino acids in different parts form weak bonds with each other. The shape of a protein is often critical for its function.
Possibly no other solid has been studied so much for the purpose of understanding small-particle infrared surface modes than MgO. The reason for this may in part be the ease with which small, highly crystalline cubes of MgO are generated by simply burning magnesium ribbon in air. Genzel (1974) has surveyed much of the experimental and theoretical work. [Pg.365]


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See also in sourсe #XX -- [ Pg.70 ]




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