Structural siding

Figure 21. Molecular structures (side views) of (a) dication salt 262+SbF6 and (b) dication salt 272+SbF6. The anions are omittedfor clarity. 

On the structural side, the range of stoichiometries, virtually without the complication of nonstoichiometry, has led to well-defined structure types, again, in many cases, with a challenge in technique for the investigator. Some of the simpler structures have been known for... 

Figure 7.19 C/s-ditopic cavitand complex 47 and its crystal structure (side view). Reproduced with permission from Ref. [57].

Domagala JM. Review Structure-activity and structure—side-effect relationships for the quinolone antibacterials. 

This anti-ulcer drug has some obvious similarities to Tagamet, and some differences too. Here are the two structures side-by-side. 

Fig. 4.3. Representative structures at the global-minimum free-energy state ((a) GM) and the two local-minimum states ((b) LM1 and (c) LM2). As for the peptide structures, besides the backbone structure, side chains of only Glu -2, Phe-8, Arg+-10, and His+-12 are shown in ball-and-stick model...

Figure 8.2.2 Single Crystal X-Ray Diffraction Structures (Side Views) of the Bis-HCl (8.13b, left) and Tetrakis-HC104 (8.13c, right) Salts of Octaphyrin-(2.1.0.1.2.1.0.1).

Although quinone structures and short, non-covalent contacts between quinones and proteins are available from X-ray diffraction structures, analogous information for the quinoidal radicals usually must be inferred indirectly from spectroscopic data. The primary spectroscopic methods used to infer the structures, side-chain conformations, and intermolecular contacts of quinoidal... 

Figure 5 Eutectic micro structure of the system H20-NaCl in which can be found both complex regular structure (sides) and the angular, branching structure associated with "irregidar morphology (center). The light phase in the CSEM/SEI is hydrohalite and the dark, recessed phase is ice-L...

The simplest way to pack a pair of adjacent helices is to place them antiparallel to one another connected by a short loop. A frequently encountered domain structure in proteins is a bundle of four parallel and antiparallel helices with their long axes aligned around a central hydrophobic core. The helices are arranged in such a way that helices that are adjacent in the amino acid sequence are also adjacent in the three-dimensional structure. Side chains from all four helices are buried in the middle of the bundle, where they form a hydrophobic core. This is illustrated by myohaemerythrin (Figure 3.15a), a nonhaem oxygen transport protein found in marine worms. 

Hooft, R. W. W., Sander, C.,Vriend, G., Verification of protein structures side-chain planarity, J. Appl. Crystallogr. 1996, 29, 714-716. 

Fig. 16. Schematic illustration of the zinhlende compound semiconductor surface structure (side view). The labeling convention is that of Duke (1990).

Fig. 17. Schematic illustration of the epitaxial continued lattice structure (ECUS) for adsorption on zinblende compound semiconductor surfaces structure (side view).

The crystal structure side-chains in contact with the peptide are shown in blue ball-and-stick figures, while the model side-chains are shown in yellow. Crystal structure Arg296 is shown in red and model structure Arg296 is shown in green, with a hydrogen bond depicted by dotted lines to Asp at PI. ... 

By ring structure. They may be further classified by structural side chain group. The various ring structures and their associated side chain groups give an indication of both antipsychotic potency and the type and degree of adverse effects (see Table). 

Figure 22 (a) Cross-sectional schematic diagrams of OLED structures (side view) (top) single layer, (middle) single heterostructure and (bottom) double heterostructure. ITO = indium-tin-oxide. The electrodes are typically 1,000-2,000 A thick. The sum of the organic layer thicknesses are <2,000 A. (b) Ideal energy level diagrams for each of the device structures. 

Figure 1.29 Alternative cartoon depictions of proteins, (a) surface display structure of small metal rich protein cytochrome c (horse heart) (pdb Ihrc) showing Van der Waal s surface coloured for positive charge (blue) and for negative charge (red). Ball and stick representations of iron-porphyrin macrocycle (prosthetic group) are shown (red) for each subunit with central iron ion rendered as Van der Waals sphere (light blue) (b) CPK structure of cytochrome c in which all polypeptide atoms are rendered as Van der Waals spheres (purple). Porphryin and iron ion are shown as in Fig. 1.28 (c) schematic display structure (top view) of parallel a/p-protein triose phosphate isomerase (chicken muscle) (pdb Itim) with a-helix shown as cylinders (red), 8-strands as arrowed ribbons (light blue), loop structures (random coil) as rods (light grey) (d) schematic display structure (side view) of triose phosphate isomerase, otherwise as for (c).

See Figure 4.2 for a hydrogen bond that is part of the a-helix (secondary structure). See Figure 4.13 for a hydrogen bond that is part of tertiary structure (side-chain hydrogen bonding). 

Figure 17.2. The structures (side view, upper figure top view, below) of a silicide (left) and silane (right), as predicted by DFTB calculations. From the side view, the puckered structure of the layer is clearly visible. (Taken from ref.

Figure 17.5. Structure (side and top views) of a siloxene layer as predicted by our DFTB method. The OH-groups above and the hydrogens below the silicon "backbone" layer can be seen clearly, as can the puckered structure. (Taken from ref 1).

Fig. 3.12 Two views of the normal tellurium crystal structure, side view (a) and view along the chain direction (b).

Fig. 6 Experimental morphology diagram for PS- -P4VP SINPATs. Squares indicate polymers that form an island structure, circles polymers forming a ribbon structure, and the triangle the polymer that forms both island and ribbon structures side by side...

Pumping Iron by Changing the Pressure Using Model Proteins with Aromatic (Large Oil-like Ring Structures) Side Chains... 

The shape of the etchable feature affects etch rate [6]. Holes of 5 pm in diameter are etched more slowly than trenches 5 pm wide. This is again related to reactant transport inside the microstructures. Making narrow structures side by side with large features, e.g., a pillar filter and a liquid reservoir or sniffer holes in a microreactor, results in larger areas being deeper than the small ones. 

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