Multidomain structures

Proteins may have multiple domains but the different domains of these proteins have never been seen independently of each other, therefore accurate determination of their boundaries is not possible and perhaps not meaningful. 

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Figure 1. Schematic diagram of a hysteresis curve for a typical ferromagnet showing magnetization (a) as a function of the applied magnetic field (H) Saturation magnetization Is Indicated by Os- Inset shows the multidomain structure and subdomain superparamagnetlc clusters.

Because of the preceding properties, our profile procedure appears to produce highly sensitive and specific common pattern representations from limited numbers of defining sequences compared with other current methods (Figs. 5 and 7). This was shown by the construction of such profiles from more than 50 completely unrelated functional families. In more than 90% of the families, the sensitivity and specificity are more than 98%. This is also supported by the repeated sampling study of the complex bacterial transcription initiation factors. Finally, these methods allow for the localized recognition of entire domains within multidomain structures, as seen in Fig. 6. 

The termination module of surfactin synthetase is a 144 kDa four-domain enzyme responsible for the incorporation of the final amino acid (L-Leu) into the surfactin peptide and subsequent cyclization of the resulting product. The structure of the TE domain of this construct was previously solved. In the recently determined 2.6 A X-ray structure of the C-A-PCP-TE construct, the entire protein chain is evident in the electron density maps. " " The structural folds of the individual domains in this module are similar to structures of monomeric domains (Figure 13). The deviations observed in this multidomain structure include a slight difference in the hinge region of C domain subdomains and an orientation of the subdomains of the A domain that is not consistent with the open or closed conformations previously described. The A domain contains... 

Single crystal and neutron diffraction measurements have recently revealed that K2CuF4 possesses a multidomain structure due to displacements of F atoms96, 975. The symmetry of the compound has been deduced to be orthorhombic (D -Bbcm, with a = b = 5.87 A, c = 12.75 A)975 rather than tetragonal. This result is not supported by recent EPR works2745. F displacement is similar to that found in KCuF3 and is attributed to the two possible orientations of Cuu eg orbitals. 

For a low-angle step (6> < 45°, i.e. R < 1), the situation is just the opposite. The area of the facets parallel to the flat surface dominates. Consequently, the orientation of the film does not change across the step. In the critical case of a 45° step, the ratio = 1. Both growth directions are equally favorable and this results in a zigzag multidomain structure with 90° boundaries. 

Sasaki, M. and Yamada, Y. (1987) The laminin B2 chain has a multidomain structure homologous to the B1 chain. J. Biol. Chem. 262 17111-17117. 

Coercive field is usually independent of the length, but is dependent on the diameter of nanowire (coercive field decreases with increase in diameter). Such increase in coercive field [116-118] can be attributed to the multidomain structures at higher diameter. 

The human factor V amino acid sequence deduced from the cDNA sequence (II) contains a signal sequence of 28 amino acids and the mature procofactor of 2196 amino acid residues. The amino acid sequence shows that factor V has a multidomainal structure that is similar to factor Vlll. The different domains can be defined as AI, between residues I-3I7 A2, from residues 318-663 B, from residues 664-1545 A3, from residues 1546-1883 Cl, from residues 1884-2036, and C2, from residues 2037-2196. As discussed previously, human factor V and factor VIII show 21 to 44% homology with ceruloplasmin in the A domains. 

The multidomain structure of PrAlOs was observed in the very first measurements of the Pr NMR at liquid helium temperatures (Konov and Teplov 1977). When a sample is placed within a cryostat in such a manner that a radiofrequency field Hi is oriented along a tetragonal axis, a spectrum related to domains oriented along H is observed (here yj < yj, see table 13). The spectral lines are characterized by large width and low intensity. 

Summarizing, most biomineralization proteins have a multidomain structure and can often be glycosylated by hydrophilic and often acidic polysaccharides, which also can form the domains interacting with the mineral. 

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