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Structural mode, coloration

Chandrasekhar et al. [67, 916] described a number of sealed, liquid- and solid-electrolyte devices based on poly(aromatic amines) similar in structure to P(ANi) and poly (diphenyl amine), operating in 2- as well as 3-electrode mode. Color changes were from glass-clear transparent to dark green-blue-black. Figs. 20-7(a-c show spectroelectrochemical characterization data for some of these. Figs. 20-8(a.b> show chronovoltabsorptometry data for solid state devices. [Pg.551]

In order to represent 3D molecular models it is necessary to supply structure files with 3D information (e.g., pdb, xyz, df, mol, etc.. If structures from a structure editor are used directly, the files do not normally include 3D data. Indusion of such data can be achieved only via 3D structure generators, force-field calculations, etc. 3D structures can then be represented in various display modes, e.g., wire frame, balls and sticks, space-filling (see Section 2.11). Proteins are visualized by various representations of helices, / -strains, or tertiary structures. An additional feature is the ability to color the atoms according to subunits, temperature, or chain types. During all such operations the molecule can be interactively moved, rotated, or zoomed by the user. [Pg.146]

Figure 10.5 Comparison of the sequence-specific binding to DNA of six different zinc fingers. Residues in the N-terminus of the a helix in the finger regions are numbered 1 to 6. The residue immediately preceding the a helix is numbered -1. Amino acid residues and nucleotides that make sequence-specific contacts are colored. In spite of the structural similarities between the zinc fingers and their overall mode of binding, there is no simple rule that governs which bases the fingers contact. Figure 10.5 Comparison of the sequence-specific binding to DNA of six different zinc fingers. Residues in the N-terminus of the a helix in the finger regions are numbered 1 to 6. The residue immediately preceding the a helix is numbered -1. Amino acid residues and nucleotides that make sequence-specific contacts are colored. In spite of the structural similarities between the zinc fingers and their overall mode of binding, there is no simple rule that governs which bases the fingers contact.
Fig. 8.12 Experimental validation of the predicted conformation and the actual binding mode of compound 43. The X-ray structure is overlaid with its calculated counterpart (colored in orange). Fig. 8.12 Experimental validation of the predicted conformation and the actual binding mode of compound 43. The X-ray structure is overlaid with its calculated counterpart (colored in orange).
Many chemical processes of undoubted antiquity, such as dyeing, soapmaking, and various metallurgical skills, must have required the ability to identify the correct raw materials or ingredients, and thus represent the application of an early form of analytical chemistry. It is likely, however, that this took the form of experience rather than direct analysis, in much the same way as a skilled mineralogist can identify hundreds of mineral species by eye, using indicators such as color, shape, mode of occurrence, and mineral associations, without resorting directly to chemical or structural analytical procedures. The earliest analytical test that we know of is that used to... [Pg.39]

Fluorescent labeling of cDNA can be a potential source of technical variability. In a typical two-color experiment, fluorescently labeled cDNA probes are transcribed from separate mRNA populations (e.g., cerebral ischemia versus sham). One set of cDNA probes is labeled with one fluorescent dye (typically Cy5) and the second set with a different fluorescent dye (Cy3). A number of methods for making labeled cDNA from the RNA samples have been tested and reviewed (Stears et al., 2000 Vernon et al., 2000 Li et al., 2002) and a number of potential sources for variation must be appreciated. First, the molecular structure of the fluorescent dyes used in making labeled cDNA can affect efficiency of dye incorporation. Second the mode of dye incorporation (direct verses indirect labeling) can affect subsequent hybridization kinetics (Stears... [Pg.396]

Figure 2 shows a global alignment of selected thionin sequences. The background color for a given residue indicates the degree of conservation of that residue in a particular position in the sequence. It is clear that thionins are highly conserved over different species. Based on their conserved sequences and similar three-dimensional structures it is reasonable to assume a common mode of action for all thionins. [Pg.260]

Fig. 3 a Structural transitions in BaTiOs according to the displacive scenario involving the freezing of the soft TO lattice mode (Cochran 1960) [3]. b Strnctnral transitions in BaTiOs according to the order-disorder scenario. Different Ti ion colors denote different occupancies (Chaves et al. 1976) [18]... [Pg.55]

Sodium nitroprusside was first prepared and investigated in the middle of the nineteenth century, and a comprehensive summary of the earlier chemical investigations has been published (17). Up to 1910-1930, the addition reactions of bases to NP were explored, involving the characterization of colored intermediates (e.g., with SH-, SR-, and SO3 ), useful for analytical purposes. The hypotensive action of NP was first demonstrated in 1929, and a considerable research effort has attempted to establish the mode of action of NP and its metabolic fate. Questions still arise on the mechanism of NO release from NP in the biological fluids, and we refer to them below. New accounts dealing with modern structural and reactivity issues associated with the coordination of nitrosyl in NP and other complexes have appeared (18-20). From the bioinorganic and environmental viewpoint, nitrosyl iron complexes have been studied with... [Pg.64]

The crystal structure of the cyclophilin-CsA-calcineurin ternary structure has yet to be resolved but the ternary structure formed by rapamycin-mediated interactions between FKBP12 and the 12-kDa fKBP-rapamycin binding (FRB) domain of the 289-kDa FRAP protein has been determined with 2.7 A resolution (Choi et al, 1996), which has more recently been refined to 2.2 A resolution (Liang et al, 1999). The structure of this complex is shown in Fig. 6 (see color insert). Several similarities as well as differences in the overall mode of interaction can be seen relative to what is observed with the FKBP-FK506-cal-cineurin structure. As was seen with the FKBP-FK506 calcineurin ternary complex, there are no overall gross conformational changes... [Pg.278]


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See also in sourсe #XX -- [ Pg.299 ]




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Color modes

Coloration, modes

Modes structure

Structural color

Structurally colored

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