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Active topology

Microreactors find new niches, Achema Daily/Chemical Engineering, June 1997 Conclusions on IMRETl micro-reactor exhibitors at ACHEMA 1997 expert opinions industry s commitment general advantages of micro flow views on commercialization extended list of leading institutes and companies activities topological approach numbering-up [226],... [Pg.89]

Suenaga, K., Wakabayashi, H., Koshino, M., Sato, Y.> Urita, K., lijima, S. (2007). Imaging active topological defects in carbon nanotubes. Nature Nanotechnology, 2, 358-360. [Pg.864]

Figure 4.19 Schematic and topological diagrams for the structure of the enzyme carboxypeptidase. The central region of the mixed p sheet contains four adjacent parallel p strands (numbers 8, 5, 3, and 4), where the strand order is reversed between strands 5 and 3. The active-site zinc atom (yellow circle) is bound to side chains in the loop regions outside the carboxy ends of these two p strands. The first part of the polypeptide chain is red, followed by green, blue, and brown. (Adapted from J. Richardson.)... Figure 4.19 Schematic and topological diagrams for the structure of the enzyme carboxypeptidase. The central region of the mixed p sheet contains four adjacent parallel p strands (numbers 8, 5, 3, and 4), where the strand order is reversed between strands 5 and 3. The active-site zinc atom (yellow circle) is bound to side chains in the loop regions outside the carboxy ends of these two p strands. The first part of the polypeptide chain is red, followed by green, blue, and brown. (Adapted from J. Richardson.)...
Figure 11.10 Topological diagram of the two domains of chymotrypsin, illustrating that the essential active-site residues are part of the same two loop regions (3-4 and 5-6, red) of the two domains. These residues form the catalytic triad, the oxyanion hole (green), and the substrate binding regions (yellow and blue) including essential residues in the specificity pocket. Figure 11.10 Topological diagram of the two domains of chymotrypsin, illustrating that the essential active-site residues are part of the same two loop regions (3-4 and 5-6, red) of the two domains. These residues form the catalytic triad, the oxyanion hole (green), and the substrate binding regions (yellow and blue) including essential residues in the specificity pocket.
Figure 13.4 Schematic diagram (a) and topology diagram (b) of the polypeptide chain of cH-ras p21. The central p sheet of this a/p structure comprises six p strands, five of which are parallel a helices are green, p strands are blue, and the adenine, ribose, and phosphate parts of the GTP analog are blue, green, and ted, respectively. The loop regions that are involved in the activity of this protein are red and labeled Gl-GS. The Gl, G3, and G4 loops have the consensus sequences G-X-X-X-X-G-K-S/T, D-X-X-E, and N-K-X-D, respectively. (Adapted from E.R Pai et al., Nature 341 209-214, 1989.)... Figure 13.4 Schematic diagram (a) and topology diagram (b) of the polypeptide chain of cH-ras p21. The central p sheet of this a/p structure comprises six p strands, five of which are parallel a helices are green, p strands are blue, and the adenine, ribose, and phosphate parts of the GTP analog are blue, green, and ted, respectively. The loop regions that are involved in the activity of this protein are red and labeled Gl-GS. The Gl, G3, and G4 loops have the consensus sequences G-X-X-X-X-G-K-S/T, D-X-X-E, and N-K-X-D, respectively. (Adapted from E.R Pai et al., Nature 341 209-214, 1989.)...
Active power factor correction circuits can take the form of nontransformer isolated switching power supply topologies, such as buck, boost, and buck/boost. The buck topology in Figure C-3 produces an output dc voltage lower than found at its input, whenever the PFC stage is operating (F > Fom). In other... [Pg.220]

Structurally Dynamics CA. Most of the CA that we will encounter throughout this book (indeed, most that are currently being studied ) assume that the underlying lattice remains a passive and static object. The lattice is thus typically an arena for activity, not an active participant in the dynamics. What if the lattice were somehow made an integral part of the dynamics That is to say, what if the topology - the sites and connections among sites -- evolved alongside the value states Structurally dynamic CA are discussed in Chapter 8. [Pg.18]

From the active site topology it seems that there is room for substrate flexibility. Indeed, experiments with the closely related P450eryF have demonstrated that some substitutions within the macrolactone ring of the substrate are possible [28] for example, reduction of the C9 oxo to the hydroxy group is well tolerated. However, any changes with impact on the overall confonnation of the substrate, thus changing the trajectory between the reactive C-H bond and the iron-bound oxy-... [Pg.361]

Transmembrane Signaling. Figure 2 Membrane topology of receptors that are associated with effector proteins. Upon binding to their cognate ligands (cyan), receptor proteins without intramolecularly linked effector domain couple via transducer proteins (yellow) to or directly recruit and activate effector proteins (red). Notch receptors release their transducer domains upon proteolytic cleavage, a, p and y stand for G-protein a-, p- and y-subunits, respectively. [Pg.1239]


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See also in sourсe #XX -- [ Pg.578 ]




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Quantitative structure-activity relationship topological indices

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