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Backbone schematic drawing

Fig. XV-16. A schematic drawing of the arrangement of polyglutamates having alkyl side chains in an LB film. The circles represent the rodlike polyglutamate backbone oriented perpendicular to the page the wiggly lines are the alkyl sidechains. (From Ref. 182.)... Fig. XV-16. A schematic drawing of the arrangement of polyglutamates having alkyl side chains in an LB film. The circles represent the rodlike polyglutamate backbone oriented perpendicular to the page the wiggly lines are the alkyl sidechains. (From Ref. 182.)...
Figure 7.1 Schematic drawing of B-DNA. Each atom of the sugar-phosphate backbones of the double helix is represented as connected circles within ribbons. The two sugar-phosphate backbones are highlighted by orange ribbons. The base pairs that are connected to the backbone are represented as blue planks. Figure 7.1 Schematic drawing of B-DNA. Each atom of the sugar-phosphate backbones of the double helix is represented as connected circles within ribbons. The two sugar-phosphate backbones are highlighted by orange ribbons. The base pairs that are connected to the backbone are represented as blue planks.
Fig. 46. Characteristics of the packing arrangement in unhydrated 1 imidazole with a separate schematics emphasizing the central loop topology lu) (H-bonds are indicated as broken lines backbone H atoms are omitted O atoms dotted N atoms hatched the hatched segments in the schematic drawing signify the imidazole rings)... Fig. 46. Characteristics of the packing arrangement in unhydrated 1 imidazole with a separate schematics emphasizing the central loop topology lu) (H-bonds are indicated as broken lines backbone H atoms are omitted O atoms dotted N atoms hatched the hatched segments in the schematic drawing signify the imidazole rings)...
Fig. 5 Chemical structure (a), absorption (a) and emission (b) spectra of POWT in different buffer solutions pH 2 (open diamond), pH 5 (open square), pH 8 (triangle) and pH 11 (x).(c) The charge of the zwitter-ionic side chain, schematic drawing of proposed backbone conformations and optical properties of POWT at different pH [9]... Fig. 5 Chemical structure (a), absorption (a) and emission (b) spectra of POWT in different buffer solutions pH 2 (open diamond), pH 5 (open square), pH 8 (triangle) and pH 11 (x).(c) The charge of the zwitter-ionic side chain, schematic drawing of proposed backbone conformations and optical properties of POWT at different pH [9]...
Fig. 1. Schematic drawing of the polypeptide backbone of ribonuclease S (bovine pancreatic ribonuclease A cleaved by subtilisin between residues 20 and 21). Spiral ribbons represent a-helices and arrows represent strands of /3 sheet. The S peptide (residues 1-20) runs down across the back of the structure. Fig. 1. Schematic drawing of the polypeptide backbone of ribonuclease S (bovine pancreatic ribonuclease A cleaved by subtilisin between residues 20 and 21). Spiral ribbons represent a-helices and arrows represent strands of /3 sheet. The S peptide (residues 1-20) runs down across the back of the structure.
Fig. 14. Schematic drawing of the backbone of an all-helical tertiary structure domain 2 of thermolysin. Fig. 14. Schematic drawing of the backbone of an all-helical tertiary structure domain 2 of thermolysin.
Fig. 23. Schematic drawing of the backbone of flavodoxin, a protein in which a parallel 0 sheet is the dominant structural feature. The sheet (represented by arrows) is shown from one edge, so that the characteristic twist can be seen clearly. Fig. 23. Schematic drawing of the backbone of flavodoxin, a protein in which a parallel 0 sheet is the dominant structural feature. The sheet (represented by arrows) is shown from one edge, so that the characteristic twist can be seen clearly.
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.
Fig. 87. Myohemerythrin as an example of an up-and-down helix bundle, (a) a-Carbon stereo (b) schematic drawing of the backbone structure, from the same viewpoint as in a. Fig. 87. Myohemerythrin as an example of an up-and-down helix bundle, (a) a-Carbon stereo (b) schematic drawing of the backbone structure, from the same viewpoint as in a.
FlC. 89. Hemoglobin (fi subunit) as an example of a Greek key helix bundle, (a) a-Carbon stereo (b) schematic drawing of the backbone as two perpendicular layers of a-helices (shown here as cylinders) (c) schematic drawing of the backbone as a Greek key helix bundle (from the same viewpoint as in a) (d) schematic end-on view of the hemoglobin helix bundle, to show that it is a slightly flattened cylinder in cross section (die C-D loop is shown dashed because it would cover part of the cylinder). [Pg.286]

Fig. 4. Schematic drawing showing inhibitors of thermolysin and their interactions with the zinc atom and with a backbone carbonyl oxygen. Attraction occurs where X = NH, forced repulsion where X = O or CHi. Fig. 4. Schematic drawing showing inhibitors of thermolysin and their interactions with the zinc atom and with a backbone carbonyl oxygen. Attraction occurs where X = NH, forced repulsion where X = O or CHi.
Figure 7-17 The structure of insulin. (A) The amino acid sequence of the A and B chains linked by disulfide bridges. (B) Sketch showing the backbone structure of the insulin molecule as revealed by X-ray analysis. The A and B chains have been labeled. Positions and orientations of aromatic side chains are also shown. (C) View of the paired N-terminal ends of the B chains in the insulin dimer. View is approximately down the pseudo-twofold axis toward the center of the hexamer. (D) Schematic drawing showing packing of six insulin molecules in the zinc-stabilized hexamer. Figure 7-17 The structure of insulin. (A) The amino acid sequence of the A and B chains linked by disulfide bridges. (B) Sketch showing the backbone structure of the insulin molecule as revealed by X-ray analysis. The A and B chains have been labeled. Positions and orientations of aromatic side chains are also shown. (C) View of the paired N-terminal ends of the B chains in the insulin dimer. View is approximately down the pseudo-twofold axis toward the center of the hexamer. (D) Schematic drawing showing packing of six insulin molecules in the zinc-stabilized hexamer.
Fig. 17. A schematic drawing of the course of the polypeptide backbone of yeast hexokinase. From Anderson et al. (74). Reprinted with permission of Academic Press. Fig. 17. A schematic drawing of the course of the polypeptide backbone of yeast hexokinase. From Anderson et al. (74). Reprinted with permission of Academic Press.
Fig. 36 Schematic drawing of a DNA molecular wire in contact with a dissipative environment. The central chain (extended states) with N sites is connected to semiinfinite left (L) and right (R) electronic reservoirs. The bath only interacts with the side chain sites (c), which we call for simplicity backbone sites, but which collectively stay for non-conducting, localized electronic states. The Hamiltonian associated with this model is given by Eqs. (443), (444), and (445) in the main text. Fig. 36 Schematic drawing of a DNA molecular wire in contact with a dissipative environment. The central chain (extended states) with N sites is connected to semiinfinite left (L) and right (R) electronic reservoirs. The bath only interacts with the side chain sites (c), which we call for simplicity backbone sites, but which collectively stay for non-conducting, localized electronic states. The Hamiltonian associated with this model is given by Eqs. (443), (444), and (445) in the main text.
Figure 17. Schematic diagrams of some representative topologically chiral proteins.79 (a) Condensed schematic drawing of the L subunit of the quinoprotein TV-MADH. The looped line represents the polypeptide backbone with N and C terminals. Cysteine (or half-cystine) residues are numbered, and their a-carbons are indicated by filled circles. Intrachain disulfide bonds are shown as dashed lines joining a pair of filled circles. The heavy line symbolizes an intrachain cofactor link, (b) Chromatium high potential iron protein (HiPIP), one of several Fe4S4 cluster-containing proteins, (c) Toxin II from the scorpion Androctonus australis Hector. Reprinted with permission from C. Liang and K. Mislow, J. Math. Chem. 1994,15,245. Copyright 1994, Baltzer Science Publishers. Figure 17. Schematic diagrams of some representative topologically chiral proteins.79 (a) Condensed schematic drawing of the L subunit of the quinoprotein TV-MADH. The looped line represents the polypeptide backbone with N and C terminals. Cysteine (or half-cystine) residues are numbered, and their a-carbons are indicated by filled circles. Intrachain disulfide bonds are shown as dashed lines joining a pair of filled circles. The heavy line symbolizes an intrachain cofactor link, (b) Chromatium high potential iron protein (HiPIP), one of several Fe4S4 cluster-containing proteins, (c) Toxin II from the scorpion Androctonus australis Hector. Reprinted with permission from C. Liang and K. Mislow, J. Math. Chem. 1994,15,245. Copyright 1994, Baltzer Science Publishers.
Figure 6. Schematic drawing of the a-carbon backbone of one subunit of Eco RI endonuclease and both strands of DNA in the complex. (Reproduced with permission from Ref. 13. Copyright 1986 American Association for the Advancement of Science.)... Figure 6. Schematic drawing of the a-carbon backbone of one subunit of Eco RI endonuclease and both strands of DNA in the complex. (Reproduced with permission from Ref. 13. Copyright 1986 American Association for the Advancement of Science.)...
Fig. 3. Schematic drawing of the backbone conformation of RNase Tl, coinplexed with giianosine 2 -phosphatc. The positions ol the ci.v-prolines (Pio.39 and Pro55). as well as the trnn.t-prolines (ProfiO and Pro73) arc intlit aied. Drawing courtesy of Udo Heinemann. Berlin. Fig. 3. Schematic drawing of the backbone conformation of RNase Tl, coinplexed with giianosine 2 -phosphatc. The positions ol the ci.v-prolines (Pio.39 and Pro55). as well as the trnn.t-prolines (ProfiO and Pro73) arc intlit aied. Drawing courtesy of Udo Heinemann. Berlin.
Fig. 2. Stereo views of the structure of the bovine HSC70 ATPase fragment with bound MgADP and P. (A) C carbon atom backbone. (B) Schematic drawing cylinders represent a and 3 m helices arrows represent /3 strands. Fig. 2. Stereo views of the structure of the bovine HSC70 ATPase fragment with bound MgADP and P. (A) C carbon atom backbone. (B) Schematic drawing cylinders represent a and 3 m helices arrows represent /3 strands.
Summary of PDHS Structure, The information concerning the solid-state structure of PDHS that has been obtained from the studies discussed in the previous sections is summarized in the schematic drawings of Figure 19, although the complete crystal structure of PDHS has not been reported yet. The unit cell of the well-ordered phase I is monoclinic, with a and b dimensions of 1.375 and 2.182 nm, respectively, and the angle y is 88° (9). The c dimension is 0.400 nm (26), which implies that the backbone has an all-trans conformation. The side chains are arranged in a direction nearly perpendicular to that of the backbone, with a nearly all- mn5 conformation. [Pg.364]

The structure at temperatures above the transition temperature (phase II), is illustrated in the schematic drawing in Figure 19b. Both the side chains and the backbone are conformationally disordered, but the side chains remain organized preferentially on planes perpendicular to the polymer chain axis. Furthermore, significant runs of trans conformations remain in the backbone (26) in such a manner that the original molecular direction is preserved as the chains pack in cylinders in a hexagonal array. The resulting... [Pg.365]

Schematic drawing of the polypeptide backbone of one of the two subunits of bovine CuZnSOD. The strands of the fi structure are shown as arrows. Schematic drawing of the polypeptide backbone of one of the two subunits of bovine CuZnSOD. The strands of the fi structure are shown as arrows.
Flu. 1. A schematic drawing of the second EF-hand calcium-binding subdomain from calbindin D9k (residues 45-74). Ligands from side-chain carboxyls are indicated in solid lines the ligand from the backbone carbonyl is indicated by a dashed line. [Pg.443]

Fig. 4. Schematic drawing of the protein backbone of a CujZnjSUperoxide dismutase subunit. The arrows indicate the eight P-strands. The copper is solvent-accessible and lies at the bottom of the active-site channel which is mainly formed by two loops. (With permission from Ref. )... Fig. 4. Schematic drawing of the protein backbone of a CujZnjSUperoxide dismutase subunit. The arrows indicate the eight P-strands. The copper is solvent-accessible and lies at the bottom of the active-site channel which is mainly formed by two loops. (With permission from Ref. )...
Figure 11.7 The double helix of DNA (a) a schematic drawing and a three-dimensional molecular model. Both representations show the bases pointing toward the center of the helix away from the sugar-phosphate backbone. Figure 11.7 The double helix of DNA (a) a schematic drawing and a three-dimensional molecular model. Both representations show the bases pointing toward the center of the helix away from the sugar-phosphate backbone.
Fig. 8.3. Schematic drawing of a polyethylene chain backbone in all-trans conformation, showing the bond length 6,the bond angle rand the structural composition of a monomer unit with the molar mass Mu.The torsion angle 6 between the first bond of a monomer unit to the first bond of the next monomer unit is shown along the connecting bond of the monomers... Fig. 8.3. Schematic drawing of a polyethylene chain backbone in all-trans conformation, showing the bond length 6,the bond angle rand the structural composition of a monomer unit with the molar mass Mu.The torsion angle 6 between the first bond of a monomer unit to the first bond of the next monomer unit is shown along the connecting bond of the monomers...
Figure 6. Schematic drawing of the polypeptide backbone of the RT heterodimer, cc- helices and P strands are represented by tubes and arrows, respectively. The p66 (upper) and p51 (lower) subunits are pulled apart in the vertical direction to make the interaction surfaces clear. Figure 6. Schematic drawing of the polypeptide backbone of the RT heterodimer, cc- helices and P strands are represented by tubes and arrows, respectively. The p66 (upper) and p51 (lower) subunits are pulled apart in the vertical direction to make the interaction surfaces clear.
In deoxyribonucleic acid (DNA), 2-deoxy-D-ribose and phosphate units alternate in the backbone. The 3 hydroxyl of one ribose unit is linked to the 5 hydroxyl of the next ribose unit by a phosphodiester bond. The heterocyclic base is connected to the ano-meric carbon of each deoxyribose unit by a /3-N-glycosidic bond. Figure 18.3 shows a schematic drawing of a DNA segment. [Pg.532]

In the top part of Figure 22.20, the sugar-phosphate backbone is in red, and the bases are shown in blue. The bottom part shows you a space-filling model. Here, your perspective is of a segment of the whole molecule. Figure 22.21 is a schematic drawing similar to Figure 22.20 (top), but its purpose is to show you how the structure of DNA leads to the mechanism for its duplication. [Pg.687]

Figure 3.5. Schematic drawing of the complete Nafion copolymer, which is composed of apolar beads (blue) and charged beads (yellow), and also a part of the atomistic level configuration of a Nafion chain. Four-monomer unit (—(CF2CF2)4—) is represented by one blue bead as the hydrophobic backbone, while the side chain (-0-CF2CF(CF3)—O—CF2CF2—SO3H) with the sulfonic acid group is expressed as one yellow bead with hydrophilic property. Figure 3.5. Schematic drawing of the complete Nafion copolymer, which is composed of apolar beads (blue) and charged beads (yellow), and also a part of the atomistic level configuration of a Nafion chain. Four-monomer unit (—(CF2CF2)4—) is represented by one blue bead as the hydrophobic backbone, while the side chain (-0-CF2CF(CF3)—O—CF2CF2—SO3H) with the sulfonic acid group is expressed as one yellow bead with hydrophilic property.

See other pages where Backbone schematic drawing is mentioned: [Pg.56]    [Pg.56]    [Pg.394]    [Pg.394]    [Pg.194]    [Pg.1627]    [Pg.347]    [Pg.190]    [Pg.736]    [Pg.736]    [Pg.714]    [Pg.693]    [Pg.264]    [Pg.1540]    [Pg.503]    [Pg.687]    [Pg.2439]    [Pg.237]   
See also in sourсe #XX -- [ Pg.54 , Pg.55 ]




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Schematic drawing

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