Diagram of interactions

Figure 7.1 Schematic diagram of interaction potential versus separation distance D for van der Waals and electrostatic double-layer interactions. The lower inset shows the collapse of the repulsive barrier as the electrolyte concentration is increased or the surface potential is decreased. At a separation distance of zero, there is an infinitely steep hard-core repulsive (or positive) interaction. (From Israelachvili 1991, reprinted with permission from Academic Press.)...

Fig. 1.5. Diagram of interactions between amino acids and organic acids that result in the buffer effect...

Figure 4.5. A schematic diagram of interactions in an aqueous metal-ligand-surface system. The parameters K refer to equilibrium constants for reactions in the direction of the arrows.

Fig. 33.4 Schematic diagram of interactions between two proteins. The two proteins in water are in (a), (c), and (e), and two proteins in KCI solution are in (b), (d), and (f). The stick labeled as H shows hydrophobic interaction. The stick labeled as E shows electrostatic interaction, (a) Two proteins in water, (b) Two proteins in KCI solution, (c) Two proteins in a short distance in water, (d) Two proteins in a long distance in KCI solution, (e) Two proteins in a long distance in water, (f) Two proteins in a short distance in KCI solution...

Figure 1 presents a general diagram of interactions in ihQ Airport Security System model. As mentioned before it is a complex hierarchical structure. One of its elements is the Screening baggage local model. It consists of two local sub-models Hand baggage... 

Figure 1 Schematic diagram of interactions that are included in current force fields. The first five interactions are included by all-atom force fields, while the others, which represent coupling interactions, are used by some but not all force fields...

Figure 6. Flow diagram of interactive substructure search system...

Figure A3.8.1 A schematic diagram of the PMF along the reaction coordinate for an isomerizing solute in the gas phase (frill curve) and in solution (broken curve). Note the modification of the barrier height, the well positions, and the reaction free energy due to the interaction with the solvent.

Figure C2.6.9. Phase diagram of charged colloidal particles. The solid lines are predictions by Robbins et al [85]. Fluid phase (open circles), fee crystal (solid circles) and bee crystal (triangles). is tire interaction energy at tire...

Fig. 4.8 Enhancement of interaction potential in a siit-shaped pore between paraliel siabs of solid. Plot of 0/0 against z/rg for various values of d/r or R/r (see text). (Reduced from a diagram of Everett and Fowl. )...

Fig. 3. Schematic diagram of a deterministic air quality model, showing the model components and interactions (1) where each of the boxes involves a large...

Figure 2.8. An x-t diagram of a piston interacting with a compressible fluid. At the origin, the piston begins moving at constant velocity, generating a shock wave. At tj, the piston stops abruptly, generating rarefaction fan. Snapshots of wave profiles at times t2 and 3 are shown.

By plotting Hugoniot curves in the pressure-particle velocity plane (P-u diagrams), a number of interactions between surfaces, shocks, and rarefactions were solved graphically. Also, the equation for entropy on the Hugoniot was expanded in terms of specific volume to show that the Hugoniot and isentrope for a material is the same in the limit of small strains. Finally, the Riemann function was derived and used to define the Riemann Invarient. 

Figure 8.6. Stress-particle velocity impedance diagram of the shock-compression and wave-interaction process leading to planar spall.

Figure 8.17 Schematic diagram of the main features of the interactions between DNA and the helix-turn-helix motif in DNA-binding proteins.

Figure 9.12 Schematic diagram of the structure of the heterodimeric yeast transcription factor Mat a2-Mat al bound to DNA. Both Mat o2 and Mat al are homeodomains containing the helix-turn-helix motif. The first helix in this motif is colored blue and the second, the recognition helix, is red. (a) The assumed structure of the Mat al homeodomain in the absence of DNA, based on Its sequence similarity to other homeodomains of known structure, (b) The structure of the Mat o2 homeodomain. The C-terminal tail (dotted) is flexible in the monomer and has no defined structure, (c) The structure of the Mat a 1-Mat a2-DNA complex. The C-terminal domain of Mat a2 (yellow) folds into an a helix (4) in the complex and interacts with the first two helices of Mat a2, to form a heterodimer that binds to DNA. (Adapted from B.J. Andrews and M.S. Donoviel, Science 270 251-253, 1995.)...

Figure 11.11 Schematic diagrams of the specificity pockets of chymotrypsin, trypsin and elastase, illustrating the preference for a side chain adjacent to the scisslle bond In polypeptide substrates. Chymotrypsin prefers aromatic side chains and trypsin prefers positively charged side chains that can interact with Asp 189 at the bottom of the specificity pocket. The pocket is blocked in elastase, which therefore prefers small uncharged side chains.

Figure 13.15 Schematic diagram of the heterotrimeric Gap complex based on the crystal structure of the transducin molecule. The a suhunit is hlue with some of the a helices and (5 strands outlined. The switch regions of the catalytic domain of Gq are violet. The (5 suhunit is light red and the seven WD repeats are represented as seven orange propeller blades. The 7 subunit is yellow. The switch regions of Gq interact with the p subunit, thereby locking them into an inactive conformation that binds GDP but not GTP.

Figure 13.17 Schematic diagram of the structure of a complex between phosducin and the transducin Gpy dimer. The p subunit of transducin is light red and the seven WD repeats are represented as seven orange blades of a propeller. The y subunit is yellow and the phosducin molecule is blue. The helical domain of phosducin interacts with Gp in the same region that Gq binds, thereby blocking the formation of a trimeric Gapy complex.

Figure 17.5 Diagram of the T4 lysozyme stmcture showing the iocations of two mutations that stabilize the protein stmcture by providing eiectrostatic interactions with the dipoles of a helices. (Adapted from H. Nicholson et al.. Nature 336 651-656, 1988.)...

Figure 17.12 Ribbon diagram of EMPl bound to the extracellular domain of the erythropoietin receptor (EBP). Binding of EMPl causes dimerization of erythropoietin receptor. The x-ray crystal structure of the EMPl-EBP complex shows a nearly symmetrical dimer complex in which both peptide monomers interact with both copies of EBP. Recognition between the EMPl peptides and EBP utilizes more than 60% of the EMPl surface and four of six loops in the erythropoietin-binding pocket of EBP.

Figure 17.15 Schematic diagrams of the main-chain conformations of the second zinc finger domain of Zif 268 (red) and the designed peptide FSD-1 (blue). The zinc finger domain is stabilized by a zinc atom whereas FSD-1 is stabilized by hydrophobic interactions between the p strands and the a helix. (Adapted from B.I. Dahiyat and S.L. Mayo, Science 278 82-87, 1997.)...

Fig. 2.31. Schematic diagram of the interactions between high-energy electrons and matter in TEM.

A more complete analysis of interacting molecules would examine all of the involved MOs in a similar wty. A correlation diagram would be constructed to determine which reactant orbital is transformed into wfiich product orbital. Reactions which permit smooth transformation of the reactant orbitals to product orbitals without intervention of high-energy transition states or intermediates can be identified in this way. If no such transformation is possible, a much higher activation energy is likely since the absence of a smooth transformation implies that bonds must be broken before they can be reformed. This treatment is more complete than the frontier orbital treatment because it focuses attention not only on the reactants but also on the products. We will describe this method of analysis in more detail in Chapter 11. The qualitative approach that has been described here is a useful and simple wty to apply MO theory to reactivity problems, and we will employ it in subsequent chapters to problems in reactivity that are best described in MO terms. I... 

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