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Gluing Spaces

Note that in particular, during such a deformation step, Am gets replaced with the simplex Am = A , and that if X was a simplex already, then Xj = Xj U = X is a simplex again. It follows that applying this [Pg.271]


Although the occurrence of six conserved cysteine residues, the spacing patterns of these residues, and possibly the pattern of disulfide structures are hallmarks of OBPs, the six-cysteine criterion alone is not sufficient to classify a certain protein as an olfactory protein [ 16]. It is important to demonstrate that an OBP is expressed only (or predominantly) in olfactory tissues. Evidence for their ability to bind odorants is also desirable, but not sine qua non. One of these criteria alone would not be enough to define a given protein as an OBP. For example, bovine serum albumin (BSA) binds to insect pheromones (Leal, unpublished data) and yet it is not an OBP because it not expressed in insect olfactory tissues. Conversely, a protein specific to antennae is not necessarily an OBP. There are other proteins that may be expressed in antennae but not in control tissues. Non-OBPs specifically accumulated in insect antennae have been previously detected (Ishida and Leal, unpublished data). Also, a glu-tathione-S-transferase has been reported to be expressed specifically in antennae of M. sexta [52]. [Pg.25]

Figure 10.4. (a) A hypothetical phase space, (b) Four copies of the hypothetical phase space, glued together at the endpoints. [Pg.307]

The influence of eutectic media on the kinetics and productivity of biocatalysts has yet to be fully elucidated. Syntheses in eutectic suspensions have been scaled up to the pilot scale in a rotating drum reactor. The bioactive peptide Na-Cbz-L-Lys(Ne-Cbz)-Gly-L-Asp(OAll)-L-Glu(OAll)OEt was synthesized via a sequential N-to-C strategy in a heterogeneous solid-liquid mixture of the substrates in the presence of chymopapain and subtilisin as well as 16-20% (w/w) water and ethanol (Gill, 2002). At substrate concentrations of around 1 m, yields of 67-74% per step at product concentrations of 0.36, 0.49, and 0.48 kg kg-1 were achieved. The corresponding space-time yields were between 0.30 and 0.64 kg (kg d)-1 and biocatalyst reuse provided productivities of 166-312 kg product (kg enzyme)-1. [Pg.362]

Conservation matrix A that corresponds to this stoichiometric matrix is obtained by calculating the null space of (v )T, as indicated by equation 6.3-4. In order to obtain a conservation matrix with identifiable rows, RowReduce is used again and the result is shown in Fig. 6.2. The figure shows that Glu, ATP, ADP, NAD0X, NADred, and Pj can be taken as the six components for glycolysis. This... [Pg.115]

Fig. 4. Positioning of helix H12 is shown in (a) for the ER LBD-E2 complex and in (b) for the ER LBD-raloxifene complex. H12 is drawn as cylinder (a = E2 complex), (b = raloxifene complex). Dotted lines indicate unmodeled regions of the structures. Hydrophobic residues located in the groove between H3 and H5 and Lys 382 (K362) are depicted in space-filling form. The locations of Asp 538, Glu 542, and Asp 545 are drawn as spheres, along with the helices that interact with H12 in the two complexes (Brzozowski etal., 1997). Fig. 4. Positioning of helix H12 is shown in (a) for the ER LBD-E2 complex and in (b) for the ER LBD-raloxifene complex. H12 is drawn as cylinder (a = E2 complex), (b = raloxifene complex). Dotted lines indicate unmodeled regions of the structures. Hydrophobic residues located in the groove between H3 and H5 and Lys 382 (K362) are depicted in space-filling form. The locations of Asp 538, Glu 542, and Asp 545 are drawn as spheres, along with the helices that interact with H12 in the two complexes (Brzozowski etal., 1997).

See other pages where Gluing Spaces is mentioned: [Pg.271]    [Pg.271]    [Pg.274]    [Pg.271]    [Pg.271]    [Pg.274]    [Pg.1123]    [Pg.1124]    [Pg.78]    [Pg.194]    [Pg.148]    [Pg.21]    [Pg.13]    [Pg.60]    [Pg.136]    [Pg.22]    [Pg.270]    [Pg.284]    [Pg.71]    [Pg.90]    [Pg.94]    [Pg.43]    [Pg.242]    [Pg.133]    [Pg.80]    [Pg.97]    [Pg.241]    [Pg.132]    [Pg.306]    [Pg.677]    [Pg.961]    [Pg.243]    [Pg.1327]    [Pg.767]    [Pg.767]    [Pg.778]    [Pg.780]    [Pg.788]    [Pg.167]    [Pg.102]    [Pg.95]    [Pg.95]    [Pg.96]    [Pg.142]    [Pg.192]    [Pg.1]    [Pg.601]    [Pg.78]   


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Gluing

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