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Domain disordered

R.W Cahn, Antiphase domains, disordered films and the ductility of ordered alloys based on Ni3 Al, Mai. Res. Soc. Symp. Proc. 81 27 (1987)... [Pg.229]

In Table 3 are collected the phase transition temperatures of C -PAMs. Table 3 shows firstly that in spite of various trials no T was to find from Cg- and Cg-PAM-T. It shows also that T remains constant at 107°C, independent of the side chain length, presumably because the side branch domain disorders from its packing as a whole domain. The experimental result that C4-PAM-T does not show T is ascribable to too low content of side branch. [Pg.483]

Amorphous domains Disordered, noncrystalline regions in the solid state of a polymer. [Pg.729]

In both cases the late stages of kinetics show power law domain growth, the nature of which does not depend on the mitial state it depends on the nature of the fluctuating variable(s) which is (are) driving the phase separation process. Such a fluctuating variable is called the order parameter for a binary mixture, tlie order parameter o(r,0 is tlie relative concentration of one of the two species and its fluctuation around the mean value is 5e(/,t) = c(r,t) - c. In the disordered phase, the system s concentration is homogeneous and the order... [Pg.732]

Surface reconstructions have been observed by STM in many systems, and the teclmique has, indeed, been used to confmn the missing row structure in the 1 x 2 reconstruction of Au(l 10) [28]. As the temperature was increased within 10 K of the transition to the disordered 1 1 phase (700 K), a drastic reduction in domain size to -20-40 A (i.e. less than the coherence width of LEED) was observed. In this way, the STM has been used to help explain and extend many observations previously made by diffraction methods. [Pg.1682]

Diffraction is not limited to periodic structures [1]. Non-periodic imperfections such as defects or vibrations, as well as sample-size or domain effects, are inevitable in practice but do not cause much difSculty or can be taken into account when studying the ordered part of a structure. Some other forms of disorder can also be handled quite well in their own right, such as lattice-gas disorder in which a given site in the unit cell is randomly occupied with less than 100% probability. At surfaces, lattice-gas disorder is very connnon when atoms or molecules are adsorbed on a substrate. The local adsorption structure in the given site can be studied in detail. [Pg.1752]

Figure 9.14 The two domains of the POU region bind in tandem on opposite sides of the DNA double helix. Both the POU-specific domain and the POU homeodomain have a helix-turn-helix motif (blue and red) which binds to DNA with their recognition helices (red) in the major groove. The linker region that joins these domains is partly disordered. (Adapted from J.D. Klemm et al.. Cell 77 21-32, 1994.)... Figure 9.14 The two domains of the POU region bind in tandem on opposite sides of the DNA double helix. Both the POU-specific domain and the POU homeodomain have a helix-turn-helix motif (blue and red) which binds to DNA with their recognition helices (red) in the major groove. The linker region that joins these domains is partly disordered. (Adapted from J.D. Klemm et al.. Cell 77 21-32, 1994.)...
The phosducin polypeptide chmn, of some 240 amino acids, is folded into two domains (Figure 13.16). The N-terminal domain is mostly a-helical and appears to be quite flexible since only a weak electron density is obtained in the structure determination. The actual path of the polypeptide chain from the end of helix to the beginning of helix Ba is tentative due to slight disorder. This region is close to serine 73 at the beginning of Ba, which also becomes disordered on phosphorylation. [Pg.265]

Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)... Figure 13.30 Ribbon diagram of the structure of Src tyrosine kinase. The structure is divided in three units starting from the N-terminus an SH3 domain (green), an SH2 domain (blue), and a tyrosine kinase (orange) that is divided into two domains and has the same fold as the cyclin dependent kinase described in Chapter 6 (see Figure 6.16a). The linker region (red) between SH2 and the kinase is bound to SH3 in a polyproline helical conformation. A tyrosine residue in the carboxy tail of the kinase is phosphorylated and bound to SH2 in its phosphotyrosine-binding site. A disordered part of the activation segment in the kinase is dashed. (Adapted from W. Xu et al.. Nature 385 595-602, 1997.)...
The molecular basis for quasi-equivalent packing was revealed by the very first structure determination to high resolution of a spherical virus, tomato bushy stunt virus. The structure of this T = 3 virus was determined to 2.9 A resolution in 1978 by Stephen Harrison and co-workers at Harvard University. The virus shell contains 180 chemically identical polypeptide chains, each of 386 amino acid residues. Each polypeptide chain folds into distinct modules an internal domain R that is disordered in the structure, a region (a) that connects R with the S domain that forms the viral shell, and, finally, a domain P that projects out from the surface. The S and P domains are joined by a hinge region (Figure 16.8). [Pg.331]

Fig. 2 illustrates the ordering process after a quench of a disordered alloy below the ordering spinodal. As it was mentioned by AC, the primary ordered domains are formed after few atomic exchanges A.t 1, while further evolution corresponds to the growth of these domains. Fig. 3 shows that in the absence of APBs the microstructure evolution under spinodal decomposition with ordering is similar to that for disordered... [Pg.104]

An ordering phase transition is characterized by a loss of symmetry the ordered phase has less symmetry than the disordered one. Hence, an ordering process leads to the coexistence of different domains of the same ordered phase. An interface forms whenever two such domains contact. The thermodynamic behavior of this interface is governed by different forces. The presence of the underlying lattice and the stability of the ordered domains tend to localize the interface and to reduce its width. On the other hand, thermal fluctuations favor an interfacial wandering and an increase of the interface width. The result of this competition depends strongly on the order of the bulk phase transition. [Pg.121]

When the bulk transition is of first order, the above mentioned arguments based on dimensionality do not apply and the would be roughening transition temperature T j may be larger than the bulk transition temperature T, in which case there is simply no roughening transition. The situation is further complicated by the wetting phenomena. When we approach T from below, the disordered phase becomes metastable and may wet the interface a large layer of disordered phase develops in between the two ordered domains. [Pg.121]

We know that another interesting phenomenon occurs when the temperature increases up to the bulk transition Tj. Previous studies have shown that the APB is wetted by the disordered phase a large layer of disordered phase develops in between the two ordered domains. In other words, the APB is splitted into two order-disorder interfaces, whose separation diverges as In(T), - T). We display in Fig. 5 the 2-dlmensional maps for T=1687 K, i.e. very close to the first-order transition. As expected, we see that the APB separates into two order-disorder interfaces. Moreover, the width of the penetrating disordered layer varies along the APB. This means that each order-disorder interface develops its own transverse fluctuations and that the APB begins to behave as two separate objects. [Pg.126]


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