Alpha schematic representation

Figure 25-11 Peptide chain of a protein coiled to form a right-handed alpha helix. Configuration of the helix is maintained by hydrogen bonds, shown as vertical dotted (or solid) lines. The helix on the left shows the detailed atom structure of the peptide chain. The helix on the right is a schematic representation without structural detail. 

Fig. 1. Schematic representation of the domain organization of Eph receptors and ephrins. SAM, sterile alpha motif.

Figure 5.2. A schematic representation of typieal alpha and beta relaxations observed from mechanical and dielectric properties. The observed relaxation temperatures increase with increasing frequency.

Figure 1 Schematic representation of the structure and polymerization of microtubules. Microtubules are cylindrical polymers (diameter, 24 nm), with a distinct molecular polarity conferred by the orientation of tubulin subunits. They exist in a dynamic equilibrium, and their assembly and disassembly depends on the reversible addition and removal of tubulin, which is a heterodimer made up of an alpha and a beta subunit, at the ends of the microtubules.

Figure 10.12 Schematic representation of alpha helix. Hydrogen bonds (dotted) connect carbonyl oxygens (red) to amino nitrogens (blue) four amino-acid units down the chain.

Gravity creaming is relatively efficient, especially in the cold (a fat content of 0.1% in the skim phase may be obtained). However, it is slow and inconvenient for industrial-scale operations. Mechanical milk separators were developed independently in the 1880s by Alpha and Laval schematic representations of a modern separator are shown in Figures 3.21 and 3.22. 

Figure 4. Schematic representation of particle paths through an alpha magnet.

FIGURE 1.28 (a) Schematic representation of alpha particle emission and (b) alpha spectrum of uranium (with a spike) after separation from other actinides in a soil sample (also... 

Figure 4 Differential O2 sensitivity of L-type Ca channel aic-subunit splice variants, (a) Schematic representation of the full-length aic-subunit of the L-type Ca channel, showing the four repeating domains, each containing six transmembrane alpha helices. The hatched box at the intracellular C-terminal indicates the only site of splice variation, (b-d) Whole-cell Ca + currents (right panels) evoked in HEK293 cells transiently transfected with aic-subunit splice variants hHT (b), rHT (c), and fHT (d) when stepping from a holding potential of —80 mV to OmV for 100 msec (C = control normoxia, H = hypoxia). In the left-hand panels are shown representative time-series plots for each splice variant before, during, and after perfusion with hypoxic solution horizontal bar indicates duration of exposure to hypoxia. Also shown pictorially in each panel is the length of the splice insert.

FIG. 19 A schematic representation of neutron capture by B , and its subsequent fission, forming a lithium ion, an alpha particle, and a high-energy photon. 

Figure 3. Schematic representation of a tetravalent MAP formed by the addition of a lysine residue to each of the two primary amine groups of a central lysine (K) residue, an airangement that provides four primary amine groups from which separate epitopes can be synthesised. The right hand schematic is an energy minimised molecular model of the trivalent lysine core indicating the alpha and epsilon amino groups to which individual epitopes are added.

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