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Let us examine some alternative results and consider the effects of the base fire dimension D. Measurements are given by Yokoi [3] for fire sources of Figure 10.9 and 20 cm radius (r0 = D/2). The temperature profiles... [Pg.313]

A mathematic appreciation of the interferogram in figure A.3 can be obtained by Fourier Transforming the step function (representing in ideal infrared source) of figure A.4. [Pg.494]

Figure 14.8 Plot of k2 against the distance of tryptophan residues from the heme in cytochrome P-450. The dotted lines in the figure show the crystallographic distances between tryptophan residues, and lines labeled with rx and show the calculated distances between the heme and different tryptophan residues using all possible values of tc2 (0.0-4.0). The point where these two lines intersect shows the k2 value for the particular residue and is indicated by the arrows. Source of figures 11.22 and 11.23 Khan, K.K., Mazumdar, S., Modi, S., Sutcliffe, M., Roberts, G.C.K. and Mitra, S. (1997). European Journal of Biochemistry, 244, 361-370. Figure 14.8 Plot of k2 against the distance of tryptophan residues from the heme in cytochrome P-450. The dotted lines in the figure show the crystallographic distances between tryptophan residues, and lines labeled with rx and show the calculated distances between the heme and different tryptophan residues using all possible values of tc2 (0.0-4.0). The point where these two lines intersect shows the k2 value for the particular residue and is indicated by the arrows. Source of figures 11.22 and 11.23 Khan, K.K., Mazumdar, S., Modi, S., Sutcliffe, M., Roberts, G.C.K. and Mitra, S. (1997). European Journal of Biochemistry, 244, 361-370.
Figure 2.8b. Fluorescence liiralion spectra of 3 ([3], 200 nM [MgCI>l, S mM [KOI], SO mM [Tris-HCI], 20 mM, at pH 8.0) in the presence of a fully complemenlaiy target DNA 5 (0.1-1 0 equiv). Upon DNA 5 binding, the decrease in the f uorescence intensity of the exclmer is accompanied witli an increase of the fluorescence intensity of the monomer. Source of figure 2.8 Fujimoto, K., Shimizu, H. and Inouye. M. 2004, J. Org. Chem. 69, 3271 -3275. Authorization of reprint accorded by the American Chemical Society... Figure 2.8b. Fluorescence liiralion spectra of 3 ([3], 200 nM [MgCI>l, S mM [KOI], SO mM [Tris-HCI], 20 mM, at pH 8.0) in the presence of a fully complemenlaiy target DNA 5 (0.1-1 0 equiv). Upon DNA 5 binding, the decrease in the f uorescence intensity of the exclmer is accompanied witli an increase of the fluorescence intensity of the monomer. Source of figure 2.8 Fujimoto, K., Shimizu, H. and Inouye. M. 2004, J. Org. Chem. 69, 3271 -3275. Authorization of reprint accorded by the American Chemical Society...
Fig. 8.17b. Normalized fluorescence intensities of 212 gM calcofluor at A.em - 435 nm as a function of the sial ic acids concentration. The intensities were corrected for the dilution and for the inner filter effect. Sources of figures 8.16 and 8.17 Albani, J. R., Sillen A., Plancke, Y. D., Coddeville, B. and Engelborghs, Y. 2000. Carbohydr. Res. 327, 333-340. Fig. 8.17b. Normalized fluorescence intensities of 212 gM calcofluor at A.em - 435 nm as a function of the sial ic acids concentration. The intensities were corrected for the dilution and for the inner filter effect. Sources of figures 8.16 and 8.17 Albani, J. R., Sillen A., Plancke, Y. D., Coddeville, B. and Engelborghs, Y. 2000. Carbohydr. Res. 327, 333-340.

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