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Folding schematic drawing

Fig. 22.6. A schematic drawing of a largely crystalline polymer like high-density polyethylene. At the top the polymer has melted and the chain-folded segments hove unwound. Fig. 22.6. A schematic drawing of a largely crystalline polymer like high-density polyethylene. At the top the polymer has melted and the chain-folded segments hove unwound.
Figure 2. Schematic drawing of a control apparatus. A laser of frequency coi is focused by lens L into a cell containing a tripling medium such as Hg vapor. Mirrors Ml and M2 are mounted inside a phase tuning cell (not shown) containing a refractive medium such as H2. The folded mirror geometry produces a pair of elliptical astigmatic foci, one of which overlaps the molecular beam (MB) at a distance zm from the beam axis. (Reproduced with permission from Ref. 62, Copyright 2006 American Physical Society.)... Figure 2. Schematic drawing of a control apparatus. A laser of frequency coi is focused by lens L into a cell containing a tripling medium such as Hg vapor. Mirrors Ml and M2 are mounted inside a phase tuning cell (not shown) containing a refractive medium such as H2. The folded mirror geometry produces a pair of elliptical astigmatic foci, one of which overlaps the molecular beam (MB) at a distance zm from the beam axis. (Reproduced with permission from Ref. 62, Copyright 2006 American Physical Society.)...
Fig. 62. A schematic drawing of the backbone of the prealbumin dimer, viewed down the 2-fold axis. Arrows represent p strands. Two of these dimers combine back-to-back to form the tetramer molecule. Fig. 62. A schematic drawing of the backbone of the prealbumin dimer, viewed down the 2-fold axis. Arrows represent p strands. Two of these dimers combine back-to-back to form the tetramer molecule.
Figure 29-2 (A) Secondary structure model for the 1542-residue E. coli 16S rRNA based on comparative sequence analysis.733 Dots indicate G U or A G pairs dashes indicate G C or A U pairs. Strongly implied tertiary interactions are shown by solid green lines. Helix numbering according to Brimacombe. Courtesy of Robin Gutell. (B) Simplified schematic drawing of type often used. (C) Positions of the A, P, and E sites on the 30S ribosomal subunit from Carter et al7° (D) Stereoscopic view of the three-dimensional fold of the 16S RNA from Thermus thermophilus as revealed by X-ray structural analysis at 0.3 nm resolution. Features labeled are the head (H), beak (Be), neck (N), platform (P), shoulder (Sh), spur (Sp), and body (Bo). (E-H) Selected parts of the 16S RNA. In (E) and (F) the helices are numbered as in (A). (F) and (H) are stereoscopic views. The decoding site... Figure 29-2 (A) Secondary structure model for the 1542-residue E. coli 16S rRNA based on comparative sequence analysis.733 Dots indicate G U or A G pairs dashes indicate G C or A U pairs. Strongly implied tertiary interactions are shown by solid green lines. Helix numbering according to Brimacombe. Courtesy of Robin Gutell. (B) Simplified schematic drawing of type often used. (C) Positions of the A, P, and E sites on the 30S ribosomal subunit from Carter et al7° (D) Stereoscopic view of the three-dimensional fold of the 16S RNA from Thermus thermophilus as revealed by X-ray structural analysis at 0.3 nm resolution. Features labeled are the head (H), beak (Be), neck (N), platform (P), shoulder (Sh), spur (Sp), and body (Bo). (E-H) Selected parts of the 16S RNA. In (E) and (F) the helices are numbered as in (A). (F) and (H) are stereoscopic views. The decoding site...
Figure 43 The structure of the iron-containing core in ferritin, (a) One way of using the phosphorus atoms to terminate the two-dimensional sheets into strips. From the stoichiometry there are nine Fe atoms per P, giving a width of —60 A. The length of the strip depends on the amount of iron in the micelle, (b) Schematic drawing of the folding of the strip into a 70 A diameter micelle (reproduced with permission from J. Am. Chem. Soc., 1979, 101, 67, American Chemical Society, Washington, DC)... Figure 43 The structure of the iron-containing core in ferritin, (a) One way of using the phosphorus atoms to terminate the two-dimensional sheets into strips. From the stoichiometry there are nine Fe atoms per P, giving a width of —60 A. The length of the strip depends on the amount of iron in the micelle, (b) Schematic drawing of the folding of the strip into a 70 A diameter micelle (reproduced with permission from J. Am. Chem. Soc., 1979, 101, 67, American Chemical Society, Washington, DC)...
Fig. 5 Schematic drawing of single crystal with regular chain folding... Fig. 5 Schematic drawing of single crystal with regular chain folding...
FIG. 2.12 Schematic drawing of the different macro-conformations possible in solid linear macromolecules, (a) Random, glassy (b) folded chain, lamellar (c) extended chain equilibrium (d) fringed micelle, mixture of (a) to (c) (after Wunderlich, 1970). [Pg.32]

Figure 1. Schematic drawing of a chain-folded polymer crystal. Figure 1. Schematic drawing of a chain-folded polymer crystal.
Fig. 3.20 CM-AFM deflection (error signal) image of POM lamella (top), height image of a collapsed PE lamella (bottom left) and friction image of the same PE crystal including schematic drawing of fold direction (bottom right). Reproduced with permission from [46] Copyright 1994. Elsevier and [48]. Copyright 1999. American Chemical Society... Fig. 3.20 CM-AFM deflection (error signal) image of POM lamella (top), height image of a collapsed PE lamella (bottom left) and friction image of the same PE crystal including schematic drawing of fold direction (bottom right). Reproduced with permission from [46] Copyright 1994. Elsevier and [48]. Copyright 1999. American Chemical Society...
When s-MDH is viewed down the dyad, as shown in Fig. 1, the first half of the polypeptide chain (ySA to ySF) is folded into a reasonably defined region. The second half of the molecule ( 2F to H) comprises the remaining part of the molecule. It should be emphasized that the distribution of atoms is continuous there is no visible bilobal structure as has been seen in other enzymes (65). The first six segments of the extended chain (pA to pF) form a twisted region of parallel sheet structure. The schematic drawing in Fig. 1 does not show this twist. The amino terminal part of the sheet (/3A, pB, and / C) is on the surface of the... [Pg.381]

Figure 32. Schematic drawing of the interlaced pattern of the six homogeneous polytypes, resulting from the nx60° rotations of the five-fold growth spirals (modified after Endo 1968). Figure 32. Schematic drawing of the interlaced pattern of the six homogeneous polytypes, resulting from the nx60° rotations of the five-fold growth spirals (modified after Endo 1968).
FIGURE 9.27 A schematic drawing of a proposed secondary structure for 16S rRNA. The intrachain folding pattern includes loops and double-stranded regions. Note the extensive intrachain hydrogen bonding. [Pg.256]

Fig. 33 Schematic drawing of probable conformations of star-shaped pol5oners in the elongational flow field (horizontal), (a) Conformation disfavors the building up of force at the core, (b) Interarm entanglement leads to stress concentration at the entanglement point, (c) Arm individualism. Each arm may have independent conformations (1) folded, (2) coiled, (3) kinked,... Fig. 33 Schematic drawing of probable conformations of star-shaped pol5oners in the elongational flow field (horizontal), (a) Conformation disfavors the building up of force at the core, (b) Interarm entanglement leads to stress concentration at the entanglement point, (c) Arm individualism. Each arm may have independent conformations (1) folded, (2) coiled, (3) kinked,...
Basically, all mitochondria consist of two membranes which surround and enclose an inner compartment containing the mitochondrial matrix. The outer membrane is usually smooth in surface contour, whereas the inner membrane is folded into a series of lamellae, the cristae. The regions of the inner membrane between the cristae are designated collectively as the inner boundary membrane. The space between the outer and inner membranes, known as the inter membrane space, is continuous with the space bounded by the membranes of the cristae. Figure 1 shows a schematic drawing of a mitochondrion. [Pg.339]

Figure 24.5 Dielectric elastomer folded actuator picture of a prototype sample and schematic drawing of the device structure. An electrical activation generates a compressive force along the axial direction. Figure 24.5 Dielectric elastomer folded actuator picture of a prototype sample and schematic drawing of the device structure. An electrical activation generates a compressive force along the axial direction.
Figure 6.6 Schematic drawing of the folded-chain lamellar model. Figure 6.6 Schematic drawing of the folded-chain lamellar model.
The X-ray crystal structure of MMOH from M. capsulatus (Bath) has been determined by Lippard et al at 2.2 A resolution [52, 53]. The X-ray diffraction data were collected at 4 The enzyme is a relatively flat molecule with approximate dimensions 60 x 100 x 200 A. The arrangement of the subunits is similar to the schematic drawing in Scheme 1. The two a-subunits contact one another and so do two P-subunits with more extensive contacts. The y-subunit lies on the outer edges of the molecule at the interface of the a-and p-subunit. The two apy protomers are related by a non-crystallographic two fold symmetry and form a heart-shaped molecule. There is a large canyon at the interface between the two aPy protomers. The secondary structure of the three subunits is primarily helical, with one small region of p-structure in the a-subunit. The a-subunit involves 18 helices and two P-hairpin motifs. The P-subunit has 12 helices. The y-... [Pg.292]

Fig. 10 (A) Schematic drawing and HR-TEM images of open and folded graphene edge nanostructures. (B) Nyquist diagrams and EIS measurements of folded (red) and open edged stacked graphene nanofibres modified electrodes 5 mM Fe(CN) " /KCl (0.1 M) (print with permission from ref. 62). Fig. 10 (A) Schematic drawing and HR-TEM images of open and folded graphene edge nanostructures. (B) Nyquist diagrams and EIS measurements of folded (red) and open edged stacked graphene nanofibres modified electrodes 5 mM Fe(CN) " /KCl (0.1 M) (print with permission from ref. 62).
Figure 2 Schematic drawing of the conformation models of a polyethylene single crystal. (A) sharp-fold, (B) switch-board and (C) loose-loop model. Reproduced with permission of Elsevier Science from Ando I, Sorita T, Yamanobe T ef a/(1985) Polymer 26 1864. Figure 2 Schematic drawing of the conformation models of a polyethylene single crystal. (A) sharp-fold, (B) switch-board and (C) loose-loop model. Reproduced with permission of Elsevier Science from Ando I, Sorita T, Yamanobe T ef a/(1985) Polymer 26 1864.
Figure 2 shows a schematic drawing of the polypeptide chain folding of subunit M subunit L is folded very similarly. Structurally similar segments in both subunits include the transmembrane helices (labeled A, B, C, D, E) and a large fraction of the polypeptide chains connecting them. In total, 216 a-carbons... [Pg.5]

Fig. 62. Electron microscopic photograph of muscle (thin section cf. schematic drawing in Fig. 63). A large number of small cross links can be distinguished between the thin filaments which are linked together (near the edges of the photograph) in the Z-line, and the thick lines. Enlargement 120,000-fold. Fig. 62. Electron microscopic photograph of muscle (thin section cf. schematic drawing in Fig. 63). A large number of small cross links can be distinguished between the thin filaments which are linked together (near the edges of the photograph) in the Z-line, and the thick lines. Enlargement 120,000-fold.
Fig. 5.10. Schematic drawing of the unfolding-folding process of RNase as a model system of the folding of the nascent chain (according to Epstein et a/., 1963). Fig. 5.10. Schematic drawing of the unfolding-folding process of RNase as a model system of the folding of the nascent chain (according to Epstein et a/., 1963).
Fig. 7. (a) Ribbon drawing of immunoglobulin domain, (b and c) Schematic of the folding topology of the immunoglobulin domain. [Pg.167]


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