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Substrate position

Figure Bl.19.12. Basic principles of SECM. (a) With ultramicroelectrode (UME) far from substrate, diflfiision leads to a steady-state current, ij, (b) UME near an insulating substrate. Flindered diflhision leads to < ij, 3D. (c) UME near a conductive substrate. Positive feedback leads to go. (Taken from [62],... Figure Bl.19.12. Basic principles of SECM. (a) With ultramicroelectrode (UME) far from substrate, diflfiision leads to a steady-state current, ij, (b) UME near an insulating substrate. Flindered diflhision leads to < ij, 3D. (c) UME near a conductive substrate. Positive feedback leads to go. (Taken from [62],...
FIGURE 2-17 Principles of SECM. (a) Tip far from the substrate surface diffusion of O leads to steady-state current. (b) Tip near a conductive substrate positive feedback of O. (c) Tip near the insulating substrate hindered diffusion of O. c = concentration a = radius of tip. (Reproduced with permission from reference 55.)... [Pg.51]

In order to achieve the enhanced strength, atomically sharp A IB interfaces are needed for the mechanism proposed by Koehler. The multilayer hlms should be deposited under a relative low temperature in order to avoid the interdiffusion between the layers. Thus, PVD techniques such as evaporation and sputtering deposition are the reasonable methods to fabricate multilayer hlms. There are several ways to achieve the alternate deposition of the composing layers A and hxed substrate position mode, repeated substrate po-... [Pg.154]

An inventory of factors affecting reactivity 8 Binding location and substrate positioning 9... [Pg.1]

Table 10.3 Effect of deviations of the standard enantioselective enzymatic conversion on the enantiomeric excess. The standard conversion is a single irreversible batch reaction in a homogeneous solution starting form racemic or prochiral substrate. (+)=positive effect, (-)=negative effect, (o)=no effect. Table 10.3 Effect of deviations of the standard enantioselective enzymatic conversion on the enantiomeric excess. The standard conversion is a single irreversible batch reaction in a homogeneous solution starting form racemic or prochiral substrate. (+)=positive effect, (-)=negative effect, (o)=no effect.
The Sharpless epoxidation is sensitive to preexisting chirality in selected substrate positions, so epoxidation in the absence or presence of molecular sieves allows easy kinetic resolution of open-chain, flexible allylic alcohols (Scheme 26) (52, 61). The relative rates, kf/ks, range from 16 to 700. The lower side-chain units of prostaglandins can be prepared in high ee and in reasonable yields (62). A doubly allylic alcohol with a meso structure can be converted to highly enantiomerically pure monoepoxy alcohol by using double asymmetric induction in the kinetic resolution (Scheme 26) (63). A mathematical model has been proposed to estimate the degree of the selectivity enhancement. [Pg.80]

For a Michaelis-Menten enzyme Rs = 81. For a sigmoidal curve, Rs <81 and the enzyme is said to exhibit positive cooperativity with respect to the substrate. Positive cooperativity implies that the substrate binding or catalytic rate, or both, increases with increasing substrate concentration more than would be expected for a simple Michaelis-Menten enzyme. If Rs >81, the enzyme is said to display negative cooperativity with respect to the substrate substrate binding or catalysis, while increasing, becomes progressively less than would be found with a simple Michaelis-Menten enzyme as substrate concentration is increased. [Pg.266]

Xu, Q., Baciou, L., Sebban, P., and Gunner, MR.. (2002) Exploring the Energy Landscape for QA- to QB Electron transfer in Bacterial photosynthetic reaction centers effect of substrate position and tail length on the conformational gating step, Biochemistry 41, 10021-10025. [Pg.226]

At the primary interaction site, M84Reco defines the amino adds that contact the substrate-like 80 s loop. A hydrophobic P4 interaction occurs between Trp-215, Tyr-99 and Phe-174 of the protease with Val-84 of eco. Gln-192 primarily mediates the P3 interaction. Previous structures of factor Xa bound to small molecule inhibitors also implicated these amino adds [29, 30]. The unusual preference at the P2 substrate position for Gly and Tyr-Trp-Phe is clarified in this structure. Tyr-99 rotates over 120° from the previous position, opening up the P2 pocket to the eco residue Thr-83, and closing down the S4 pocket. This conformational change at Tyr-99 explains the factor Xa preference for large hydrophobic P2 amino acids that was so puzzling in the initial structures. [Pg.179]

In this structure, eco defines an active site binding surface of over 1900 A, and explains the unusual kinetic results at the P2 substrate position. It also orders a... [Pg.179]

Protease is used to screen bead library for protease substrate positive beads in this fluorescent-quench assay fluoresce because the quencher is cleaved. [Pg.295]

An engineered water-soluble C4H (originally from Helianthus tuherosus) has been expressed and purified from yeast and used for H-NMR studies in order to investigate the active site and the substrate positioning. The initial placement of the cinnamate parallel to the heme was not able to explain the exclusive 4-hydroxylation of the substrate and it was suggested that the substrate has to shift during the catalytic cycle (Schoch et al, 2003). [Pg.186]

Substrate Positioning and Substrate Assisted Catalysis in the Peptidyl Transferase Center of the Ribosome... [Pg.2021]

The potential for RNA to act as a catalyst is dictated by its structure as a linear polymer of the four common ribonucleotides. Like DNA, RNA can form double stranded, antiparallel helices via traditional Watson-Crick base pairing. However, the backbone of nucleic acid is highly flexible and RNA can form complex tertiary structures that often involve non-Watson-Crick base pairing to create active site crevices for catalysis. The phosphodiester backbone is charged negatively and interacts electrostatically as well as by direct coordination with solution divalent cations. Ribose, purines, and pyrimidine bases contain both H-bond donors and acceptors that help stabilize higher-order stmcture and provide for substrate positioning, as well as participate in active site interactions. [Pg.2023]

Substrate position Immersed Immersed Immersed Immersed Remote... [Pg.167]


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See also in sourсe #XX -- [ Pg.43 ]




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