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Structure stick

C.6 Write the chemical formula of each ball-and-stick structure. See Exercise C.5 for the color code. [Pg.53]

Draw stick structures to represent each of the following molecules (a) nonane, CH3(CI l2)-CI I3 (b) cyclopropane,... [Pg.867]

Draw stick structures of the possible products for the reaction of sodium ethoxide with (a) 1-bromobutane ... [Pg.868]

Stem-Gerlach experiment The demonstration of the quantization of electron spin by passing a beam of atoms through a magnetic field, stick structure See line structure. stock solution A solution stored in concentrated form, stoichiometric coefficients The numbers multiplying chemical formulas in a chemical equation. [Pg.968]

C09-0098. Draw Lewis structures and ball-and-stick structures showing the geometries of molecules of the... [Pg.648]

C13-0038. Convert the ball-and-stick structures to line drawings and identify the functional groups in the following molecules ... [Pg.958]

Figure 22 Positioning of the Tyr8 phenol ring (colored stick structures) relative to the Ni11 (purple sphere) and its chelate ring (ball-and-stick structure). The lowest-energy representatives of conformational families 1-3 are shown in blue, green, and yellow, respectively. The phenol oxygen is a red sphere.1747... Figure 22 Positioning of the Tyr8 phenol ring (colored stick structures) relative to the Ni11 (purple sphere) and its chelate ring (ball-and-stick structure). The lowest-energy representatives of conformational families 1-3 are shown in blue, green, and yellow, respectively. The phenol oxygen is a red sphere.1747...
Fig. 1 (a) Ball and stick structure of faujasite (FAU). (b) Conventional stick drawing of faujasite (FAU). [Pg.227]

Faujasite (FAU), 226-227 ball and stick structure of, 226-227, 227/ Fluorescence correlation spectroscopy, 178-181... [Pg.366]

Figure 2 Crystal structure of PKA and conserved active site, (a) Crystal structure image of PKA (green) in complex with peptide substrate inhibitor, ATP is displayed as a ball and stick structure (blue) and Mg + Ions (orange), (b) ATP binding residues of the kinase with ATP (blue), Mg + ions (orange), and substrate (red) are shown. Figure 2 Crystal structure of PKA and conserved active site, (a) Crystal structure image of PKA (green) in complex with peptide substrate inhibitor, ATP is displayed as a ball and stick structure (blue) and Mg + Ions (orange), (b) ATP binding residues of the kinase with ATP (blue), Mg + ions (orange), and substrate (red) are shown.
FIGURE 11-41 Structures of two ABC transporters of E, coli, (a) The lipid A flippase MsbA (PDB ID 1JSQ) and (b) the vitamin B12 importer BtuCD (PDB ID 1L7V). Both structures are homodimers. The two nucleotidebinding domains (NBDs, in red) extend into the cytoplasm. In (b), residues involved in ATP binding and hydrolysis are shown as ball-and-stick structures. Each monomer of MsbA has six transmembrane helical segments (blue), and each monomer of BtuCD has ten. [Pg.402]

FIGURE 12-7 Activation of the insulin-receptor Tyr kinase by autophosphorylation. (a) In the inactive form of the Tyr kinase domain (PDB ID 11RK), the activation loop (blue) sits in the active site, and none of the critical Tyr residues (black and red ball-and-stick structures) are phosphorylated. This conformation is stabilized by hydrogen bonding between Tyr1162 and Asp"32, (b) When insulin binds to the a chains of insulin receptors, the Tyr kinase of each /3 subunit of the dimer phosphorylates three Tyr residues (Tyr"58, Tyr"62, and... [Pg.431]

FIGURE 27-17 Aminoacyl-tRNA synthetases. Both synthetases are complexed with their cognate tRNAs (green stick structures). Bound ATP (red) pinpoints the active site near the end of the aminoacyl arm. [Pg.1054]

We can see the different structural features of n-pentane, Ao-pentane, and neo-pentane more clearly by drawing the molecules in two dimensions, as shown in the middle row of Figure 12.1. Alternatively, we can represent them by the stick structures shown in the bottom row. A stick structure is a commonly used, shorthand notation for representing an organic molecule. Each line (stick)... [Pg.392]

These three hydrocarbons all have the same molecular formula. We can see their different structural features by highlighting the carbon framework in two dimensions. Easy-to-draw stick structures that use lines for all carbon—carbon covalent bonds can also be used. [Pg.393]

Honey is a mixture of the monosaccharides glucose and fructose. Glucose is a six-membered ring, and fructose is a five-membered ring. For simplicity, the stick structures introduced in Chapter 12 are shown below each molecular model. [Pg.433]

Ribbon drawing of the 238-residue green fluorescent protein showing the embedded chromophore as a ball-and-stick structure.1 Courtesy of S. James Remington. [Pg.1344]

Organic chemists commonly deal with complex molecules containing dozens of carbon and hydrogen atoms. They have found a way to report the molecular structures in a very simple way, by not showing the C and FI atoms explicitly. A stick structure represents a chain of carbon atoms... [Pg.60]

A stick structure (introduced in Section C) represents a chain of carbon atoms as a zigzag line. The end of each short line in the zigzag represents a carbon atom. Because carbon nearly always has a valence of 4 in organic compounds, we do not need to show the C—H bonds. We just fill in the correct number of hydrogen atoms mentally, as we see for methylbutane (1), isoprene (2), and propyne (3). A benzene ring is represented by a circle inside a hexagon, and we need to remember that one hydrogen atom is attached to each carbon atom. [Pg.984]

Figure 5.3 (a) Ball and stick representation of aspirin, (b) Ribbon representation of dihydrofolate reductase, (c) Mesh representation of aspirin. This representation shown simultaneously both the space fill and stick structures of the molecule, (d) Molecular dynamics representation of aspirin at 500 K. The relative movement of the atoms with time within the molecule is indicated by the use of multiple lines between the atoms... [Pg.99]

Fig. 2. A 5-HT2A-receptor model constructed from the rhodopsin crystal structure. Serotonin is shown as a space-filled structure. Magenta colored backbone traces represent modeled structures of low reliability (N-terminus, C-terminus, and i3) as well as segments generated by insertion into or deletion of rhodopsin residues (el, e2, e3, and i3 loops). Stick structures of the side chains of conserved residues (yellow), ligandbinding site residues (red), and residues involved in receptor activation are shown. (Illustration appears in color in insert that follows p. 240.)... Fig. 2. A 5-HT2A-receptor model constructed from the rhodopsin crystal structure. Serotonin is shown as a space-filled structure. Magenta colored backbone traces represent modeled structures of low reliability (N-terminus, C-terminus, and i3) as well as segments generated by insertion into or deletion of rhodopsin residues (el, e2, e3, and i3 loops). Stick structures of the side chains of conserved residues (yellow), ligandbinding site residues (red), and residues involved in receptor activation are shown. (Illustration appears in color in insert that follows p. 240.)...

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See also in sourсe #XX -- [ Pg.392 , Pg.393 ]

See also in sourсe #XX -- [ Pg.26 , Pg.835 ]

See also in sourсe #XX -- [ Pg.392 , Pg.393 ]




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