Ball and stick representation

When they were challenged by another gronp to really explain the occnrrence of the transformation, they constracted more than one ball and stick representations for each species in order to snpport the production of their model. Moreover, the students discussed their colleagues models, making it evident that they had nnderstood other models of representation. 

Fig. 18.2 Ball and stick representations of the crystal packing of (a) CsCujClj, (b) (HjNMejjCujClj and (c) (NMe4)Cu2Cl3.

Ball-and-stick representations of two forms of metasilicates, the six-Si ring of beryl left) and a portion of the linear chain of jade right). 

Ball-and-stick representation and stmctural formula common to all of the naturally occurring amino acids. 

Fig. 3.2 Superposition of E. coli and S. aureus PDF. Comparison of the overall structure of E. coli PDF (Blue, PDB code 2A18 ) and S. aureus PDF (mangenta, PDB code 2A19). The bound nickel is shown in red and His-132, His-136 and Cys-90 from E. coli PDF are shown as ball and stick representation.

Fig. 5. Ball and stick representations of [Fei2(SePh)24] in the side-on view, the carbon atoms of the phenyl rings have been omitted for clarity.

Fig. 6. Ball and stick representation of (>-[Na2FeIKS .(lls Na atoms, crosshatched spheres the Na-S bonds are drawn as dotted lines.

Fig. 7. Ball and stick representations of (a) Na C Fee[N(CH2CH20)3]6 i and (b) Cs C Fe8[N(CH2CH20)3lg +, showing the template effect of the alkaline cation.

Fig. 9. Ball and stick representations of [Ni24(OH)8(mpo)16(02CMe)24(Hmpo)i6] and trinuclear oligomer.

Fig. 15. Ball and stick representations of (a) [P4Mo6028(OH)3]9 (P4MoGOe), (b) [P4Mo6S3025(OH)3]9 (P4MogS303), (c) [P4Mo6S6022(0H)3]9- (P4Mo6S6) (d) their common polyhedral representation (e) a view of the dimeric species formed by an M2+ ion (M = Cr, Mn, Fe, Co, Ni, Zn, Cd) or a sodium cation sandwiched by two P4Mo6EG units.

Fig. 5.1. Ribbon diagram of a fluorescent protein (citrine, PDB entry 1HUI) crystal structure. The chromophore is buried in the protein s interior and shown in balls and sticks representation.

Fig. 14 Ball and stick representation of trinuclear complexes with M = Co or Mn (hydrogen atoms have been removed for simplicity). Coordination details are given separately (in the circle) where, for simplicity, we have removed aromatic rings of benzoates as well as TTF—CH=CH—py...

Fig. 8. Lck SH2 domain-peptide complex (Ac-cmF-Glu-Glu-Ile-OH, 12) revealing the twopronged plug engaging a two-holed socket 1 binding mode, reminiscent of the majority of SH2 domains (Protein Databank entry code 1BHF.PDB [118]). The protein is depicted in a Connolly surface mode, the ligand is given in a ball-and-stick representation. The cmF residue is deeply buried in its binding pocket (left)...

Fig. 2. Ball-and-stick representations of two differently oriented asparagine ladders of (A) W-arcade taken from the crystal structures of pectate lyase C (Lietzke et al., 1996) and (b) ppl-arcade taken from l DP-.V-aretylglucosamine acyltransferase (Raetz and Roderick, 1995). b, l, and so on refer to a one-letter conformational code (Fig. IOC). The ladders are viewed from within the respective /(-solenoids. The arrow shows the orientation (N- to C-terminal) of the solenoid. Oxygen atoms are in red, nitrogen in blue, and carbon in green. Dotted lines designate H-bonds of side chains (red) and inter-coil H-bonds of the polypeptide backbone (black). Except for the ladder-forming asparagines, only the backbones of the coils are shown. Panels are reprinted from Hennetin et al. (2006) with the permission of the publisher.

Fig. 3. A gallery of structures representative of the distinct /8-solenoid groups shown in Tables I and II. The /8-solenoid domains are in blue and other domains are in yellow. In the oligomeric structures, only one subunit is colored while the other ones are gray. Small ligand molecules are shown in the ball-and-stick representation and colored magenta.

Fig. 4. Representative structures of the distinct types of coil shapes, viewed along the //-solenoid axis. The structures shown are limited to two coils. The /1-strands are shown as red arrows connected by loops. The side chains are shown in the ball-and-stick representation and colored gray.

Fig. 4. The molecular structure, determined by solution NMR (James et al., 1997), of Syrian hamster 90-231 (SHa90-231) prion with ball-and-stick representation of the HI domain (SHal09-122 MKHMAGAAAAGAW). Note that two short /(-chains (SI, S2) nearly stack in the hydrogen-bonding direction. If the palindromic polyalanine region was also in a /(-conformation, there would be a three-stranded /(-sheet. The structural difference between PrPc and PrPSc is in the 90-145 domain. [Model drawn using MOLSCRIPT (Kraulis, 1991)].

Figure 4.14 The B-form of the DNA double-helix viewed along the helix axis, in a ball-and-stick representation (left) and a space-filling representation (right). (From Voet and Voet, 2004. Reproduced with permission from John Wiley Sons., Inc.)...

Ro 05-8733. The ligand is shown in a ball-and-stick representation the protein backbone is displayed by tubes connecting the C atoms. White balls along the protein backbone indicate residues for which a difference in chemical shift greater than 0.2 ppm was observed. 

Fig. 3.5. MoeB-catalyzed reaction. (A) Structure of the MoeB-MoaD heterodimer with MoaD in yellow and MoeB in red. Atoms in MoeB are shown as gray spheres representing their van der Waals radii and are rendered transparent. Residues 75 to 81 of MoaD, the AMP and sulfate molecule are shown in ball-and-stick representation. (B) Close-up stereo...

Fig. 7. Structure of the singly-bridged Au-oxo complex, 3. Top left, combination polyhedral/ball-and-stick representation right, thermal ellipsoid plot. The PO4 and WOe polyhedra (or W atom) are shown in lighter and darker gray. Bottom left. X-ray structure of the coordination polyhedron...

The standard presentation of NCP molecular models uses skeleton building blocks ball and stick representations of atoms and bonds, or secondary structural cartoon features that emphasize the a-helical nature of the histone core. While these simplifications are necessary to convey some of the character of the salient... 

See Figure 7 for the ball and stick representation of this molecule. 

There is a special and very important feature of the anticipated open nido twelve-vertex structures in Fig. 12 repetition of single Lipscomb dsd rearrangements (denoted by the two-headed arrows) monotonically allows the six skeletal atoms about the open face to rotate about the second tier of five skeletal atoms (two-tier dsd rotation). Each dsd rearrangement [85, 163) (valence bond tautomerism) recreates the same configuration and involves only the motion of two skeletal atoms (in the ball-and-stick representation) and would allow carbons, if located in different tiers, to migrate apart. Such wholesale valence bond tautomerism is known to accompany the presence of seven-coordinate BH groups, e.g., and CBjoHu 142,155). 

Schemes Combination wireframe/ball-and-stick representations of the eight multi-iron Wells-Dawson sandwich-type complexes studied in this section (taken from Ref. 1). 

Schemes Combined polyhedral/ball-and-stick representation of [Ni3Na(H20)2(AsW9034)2] -TheAs04, WOe, and NiOe polyhedra are shown in yellow, red, and green, respectively. The sodium atom is shown as a blue ball and its terminal water molecule as a red ball (taken from Ref 106).

FIGURE 7.2 The structure of quartz (a) as a ball and stick representation and (b) as linked [S104] tetrahedra. 

Figures. View ofthe packing of 49 (a) and 40 (b), showing the formation of channels along the c axis. Anions are in grey. For 40 the toluene molecules (in black) are in a ball and stick representation.

Figure 2. X-ray crystallographic structure of catenane 13 (left ball-and-stick representation right CPK representation).

Figure 23-45 (A) Some aspects of the structure of bacteriorhodopsin. Ribbon diagram with the retinal Schiff base in ball-and-stick representation. At the top the helices are labeled as in Fig. 23-41. The locations of aspartate, glutamate, and arginine residues that might carry protons during the proton pumping action are indicated. Retinal is shown attached to lysine 216.

Figure 23-49 Overall view of the DNA photolyase structure from E. coli. The ribbon traces the 471-residue chain. The bound cofactors FAD (left) and 5,10-methenyltetrahy-drofolate (right) are shown in ball-and-stick representation. From Park et al.652 Courtesy of Johan Deisenhofer.

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