Ball-and-stick structures

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

C09-0098. Draw Lewis structures and ball-and-stick structures showing the geometries of molecules of the... 

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

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). 

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

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. 

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... 

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. 

Fig. 7.2 Tlie crystal structure of mammalian Ser/Thr protein phosphatase-1, complexed with the toxin mycrocystin was determined at 2.1 A resolution. PPl has a single domain with a fold, distinct from that of the protein tyrosine phosphatases. The Ser/Thr protein phosphatase-1, is a metalloenzyme with two metal ions positioned at the active site with the help of a p-a-p-o-p scaffold. A dinuclear ion centre consisting of Mn2+ And Fe2+ g situated at the catalytic site that binds the phosphate moiety of the substrate. Ser/Thr phosphatases, PPl and PP2A, are inhibited by the membrane-permeable ocadaic acid and by cyclic hexapeptides, known as microcystins. The toxin molecule is depicted as a ball-and-stick structure. On the left and on the ri t, two different views of the same molecule are shown. Microcystin binds to three distinct regions of the phosphatase to the metaLbinding site, to a hydrophobic groove, and to the edge of a C-terminal groove in the vicinity of the active site. At the surface are binding sites for substrates and inhibitors. These ribbon models are reproduced vnth permission of the authors and Nature from ref. 9.

Figure 10.10. Comparison of the structures of HIV-P apoenzyme monomer (top, PDB code 3PHV) and the wmplex between HN-P and (32) (U-85548 bottom, PDB wde 8HVP). The inhibitor is shown as a ball and stick structure. Note the rearrangement of the flap residues Ile50 is indicated for reference. The van der Waals surface of Asp25 is shown in both structures. The flap water (red ball) is also shown between HeSO and U-85548. In the bottom structure, the locations of the N and C termini of HN-P are noted.

Fig. 2. (A) Atomic resolution STM image of a carbon tube, 35 A in diameter. In addition to the atomic honeycomb structure, a zigzag superpattern along the tube axis can be seen. (B) "Ball-and-stick" structural model of a Cg(,-based carbon tube. The upper part is closed by a Cgo hemisphere cap. (C) Structural model of a giant superpattern produced by two misoriented graphitic sheets. The carbon atoms in the first layer are shaded, and the second layer atoms are open. Between the two dashed lines, we highlight those first layer atoms with white that do not overlap with second layer atoms. Because of their higher local density of states at the Fermi level, these atoms (p-type atoms) appear particularly bright in STM images (16,21). [ results in a zigzag superpattern along the tube axis within the two white dashed lines as indicated.

The protease is a dimer of identical subunits, sliown in blue and yellow, consisting of 99 amino acids each. Notice the placement of active-site aspartic acid residues, one from each chain, which are shown as ball-and-stick structures. The flaps will close down on the binding pocket after substrate has been bound. [Drawn from 3PHV.pdb.]... 

Figure 1. Ball-and-stick structural representations of [(VO)3(SbW9033)2] (a) and [(VO)3(BiW

In a compound composed of molecules, the individual molecules move around as independent units. For example, a molecule of methane gas can be represented in several ways. The structural formula for methane (CH4) is shown in Fig. 2.16(a). The spacefilling model of methane, which shows the relative sizes of the atoms as well as their relative orientation in the molecule, is given in Fig. 2.16(b). Ball-and-stick models are also used to represent molecules. The ball-and-stick structure of methane is shown in Fig. 2.16(c). 

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