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Representation domain

The final step going from the small IRs of the little group G(k) to the IRs of G requires the theory of induced representations (Section 4.8). At a particular k in the representation domain, the left coset expansion of G on the little group G(k) is... [Pg.337]

This method of finding all the IRs of the space group G at any particular value of k in the representation domain of the BZ will now be summarized. [Pg.338]

Experts typically are able to work in several representational domains, while novices are more limited in flexibility between or among representational domains. Kozma et al. (1993) raise a critical point with regard to this use of representations that without the information that experts know, novices may construct internal representations that rely on and are constrained by the external qualities of the representation. For example, it may be that because the color stops changing in the observed representation, students develop the misconception that at equilibrium, reactions come to a stop (1993, p. 7). [Pg.232]

Fig. 14. X-ray crystal structure of full-length yeast CCS [pdb code Iqup (Lamb et al., 1999)]. (a) One monomer of yCCS is in light gray and the other is in dark gray. The cysteine residues of the MXCXXC motif in domain 1 are labeled and form a disulfide bond in each subunit. Amino acid side chains that are important in the formation of the positive patch at the dimer interface (Arg-188 and Arg-217) and the solvent-exposed Trp-183 residues of loop 6 at the center of this patch are shown in ball-and-stick representation. Domain 3 is not visible in the crystal structure (see text), (b) Stereo view of the image in (a) rotated 90° in the horizontal plane of the page and then 90° counterclockwise around an axis perpendicular to the page. The side chains that form the putative ySODl interaction surface are represented as ball-and-stick. The cysteine residues of the domain 1 MXCXXC motif are also represented in ball-and-stick. Fig. 14. X-ray crystal structure of full-length yeast CCS [pdb code Iqup (Lamb et al., 1999)]. (a) One monomer of yCCS is in light gray and the other is in dark gray. The cysteine residues of the MXCXXC motif in domain 1 are labeled and form a disulfide bond in each subunit. Amino acid side chains that are important in the formation of the positive patch at the dimer interface (Arg-188 and Arg-217) and the solvent-exposed Trp-183 residues of loop 6 at the center of this patch are shown in ball-and-stick representation. Domain 3 is not visible in the crystal structure (see text), (b) Stereo view of the image in (a) rotated 90° in the horizontal plane of the page and then 90° counterclockwise around an axis perpendicular to the page. The side chains that form the putative ySODl interaction surface are represented as ball-and-stick. The cysteine residues of the domain 1 MXCXXC motif are also represented in ball-and-stick.
For each space group there is a representation domain of the appropriate BZ (it is also called the irreducible part of the Brillouin zone), such that is equal to the... [Pg.55]

In Sect. 3.1.2 points and fines of symmetry in the Brillouin zone were defined for the case when F = F° (holosymmetric space groups, in particular 0 and D f. In the same manner the points and lines of symmetry may be defined for the point group F C F°. Then, instead of the basic domain of the BriUouin zone the representation domain is introduced. [Pg.60]

However, it is easily shown that if the mother wavelet is located in the frequency domain "around"/o (fig 8), then the wavelet a.b(t) is located around f(/a. That is to say, by the mean of the formal identification f = fata it is possible to interpret a time-scale representation as a time-frequency representation [4]. [Pg.360]

The projection of a domain plot onto its base makes a convenient two-dimensional graphical representation for describing adsorption-desorption operations. Here, the domain region that is filled can be indicated by shading the appropriate portion of the 45° base triangle. Indicate the appropriate shading for (a) adsorption up to Xa - 0.8 (b) such adsorption followed by desorption to Xd - 0.5 and (c) followed by readsorption from Xd = 0.5 to Xa = 0.7. [Pg.675]

Figure Bl.2.7. Time domain and frequency domain representations of several interferograms. (a) Single frequency, (b) two frequencies, one of which is 1.2 times greater than the other, (c) same as (b), except the high frequency component has only half the amplitude and (d) Gaussian distribution of frequencies. Figure Bl.2.7. Time domain and frequency domain representations of several interferograms. (a) Single frequency, (b) two frequencies, one of which is 1.2 times greater than the other, (c) same as (b), except the high frequency component has only half the amplitude and (d) Gaussian distribution of frequencies.
Following the discretization of the solution domain Q (i.e. line AB) into two-node Lagrange elements, and representation of T as T = Ni(x)Ti) in terms of shape functions A, (.v), i = 1,2 within the space of a finite element Q, the elemental Galerkin-weighted residual statement of the differential equation is written as... [Pg.55]

Figure 5.19 Schematic representation of a thin-layer domain between flat surfaces... Figure 5.19 Schematic representation of a thin-layer domain between flat surfaces...
Figure 3.6 Four-helix bundles frequently occur as domains in a proteins. The arrangement of the a helices is such that adjacent helices in the amino acid sequence are also adjacent in the three-dimensional structure. Some side chains from all four helices are buried in the middle of the bundle, where they form a hydrophobic core, (a) Schematic representation of the path of the polypeptide chain in a four-helrx-bundle domain. Red cylinders are a helices, (b) Schematic view of a projection down the bundle axis. Large circles represent the main chain of the a helices small circles are side chains. Green circles are the buried hydrophobic side chains red circles are side chains that are exposed on the surface of the bundle, which are mainly hydrophilic. Figure 3.6 Four-helix bundles frequently occur as domains in a proteins. The arrangement of the a helices is such that adjacent helices in the amino acid sequence are also adjacent in the three-dimensional structure. Some side chains from all four helices are buried in the middle of the bundle, where they form a hydrophobic core, (a) Schematic representation of the path of the polypeptide chain in a four-helrx-bundle domain. Red cylinders are a helices, (b) Schematic view of a projection down the bundle axis. Large circles represent the main chain of the a helices small circles are side chains. Green circles are the buried hydrophobic side chains red circles are side chains that are exposed on the surface of the bundle, which are mainly hydrophilic.
Figure 15.18 (a) Schematic representation of the path of the polypeptide chain in the structure of the class I MHC protein HLA-A2. Disulfide bonds are indicated as two connected spheres. The molecule is shown with the membrane proximal immunoglobulin-like domains (a3 and Pzm) at the bottom and the polymorphic al and a2 domains at the top. [Pg.313]

Figure 15.19 Schematic representation of the peptide-binding domain of a class I MHC protein. The al and a2 domains are viewed from the top of the molecule, showing the empty antigen-binding site as well as the surface that is contacted by a T-cell receptor. (Adapted from P.J. Bjdrkman et al.. Nature 329 506-512, 1987.)... Figure 15.19 Schematic representation of the peptide-binding domain of a class I MHC protein. The al and a2 domains are viewed from the top of the molecule, showing the empty antigen-binding site as well as the surface that is contacted by a T-cell receptor. (Adapted from P.J. Bjdrkman et al.. Nature 329 506-512, 1987.)...
Figure 17.16 Ribbon diagram representations of the structures of domain B1 from protein G (blue) and the dimer of Rop (red). The fold of B1 has been converted to an a-helical protein like Rop by changing 50% of its amino acids sequence. (Adapted from S. Dalai et al.,... Figure 17.16 Ribbon diagram representations of the structures of domain B1 from protein G (blue) and the dimer of Rop (red). The fold of B1 has been converted to an a-helical protein like Rop by changing 50% of its amino acids sequence. (Adapted from S. Dalai et al.,...
Figure 3.8. Schematic representation of the polystyrene domain structure in styrene-butadiene-styrene triblock copolymers. (After Holden, Bishop and Legge )... Figure 3.8. Schematic representation of the polystyrene domain structure in styrene-butadiene-styrene triblock copolymers. (After Holden, Bishop and Legge )...
Villermaux, J. and Devillon, J.C., 1975. Representation de la coalescence et de la redispersion des domains de segregation dans un fluide par un modele d interaction phenomenologique. In Proceedings of the second international conference of chemical reaction engineering. Amsterdam, pp. Bl-13. [Pg.325]

FIGURE 1.11 Three -dimensional spacefilling representation of part of a protein molecule, the antigen-binding domain of immunoglobulin G (IgG). Immunoglobulin G is a major type of circulating antibody. Each of the spheres represents an atom in the structure. [Pg.14]

Figure 2 Schematic representation of the domain structure of styrene-butadiene-styrene block copolymer. Figure 2 Schematic representation of the domain structure of styrene-butadiene-styrene block copolymer.
Used in conjunction with zero-to-peak (PK) terms, velocity is the best representation of the true energy generated by a machine when relative or bearing cap-data are used. (Note Most vibration monitoring programs rely on data acquired from machine housing or bearing caps.) In most cases, peak velocity values are used with vibration data between 0 and 1000 Hz. These data are acquired with microprocessor-based, frequency-domain systems. [Pg.675]

With frequency-domain analysis, the average spectmm for a machine-train signature can be obtained. Recurring peaks can be normalized to present an accurate representation of the machine-train condition. Figure 43.20 illustrates a simplified relationship between the two methods (i.e., time-domain and frequency-domain). [Pg.685]

The frequency-domain, or TFT, signature acquired at each measurement point is an actual representation of the individual machine-train component s motion at that point on the machine. Without knowing the specific location and orientation, it is difficult - if not impossible - to correctly identify incipient problems. In simple terms, the TFT signature is a photograph of the mechanical motion of a machine-train in a specific direction and at a specific point and time. [Pg.701]

Caspases. Figure 1 Schematic representation of caspase domain architecture. Illustration of all identified Homo sapiens and Mus musculus caspases. The prodomain, and the large (p20) and small (p10) subunits are proportionally depicted. [Pg.329]

Phospholipases. Figure 2 Representation ofthe domains in the major isozymes of phospholipase C (adapted from [2]). [Pg.969]

Phospholipases. Figure 3 Representation ofthe domain structure of phospholipase D1 (adapted from [4]). [Pg.969]


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See also in sourсe #XX -- [ Pg.332 ]

See also in sourсe #XX -- [ Pg.16 ]




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