Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Alignment of domains

In contrast to lamellar microdomains, where removal of defects and alignment of domains can, in principle, restore terminal behavior to G and G", even after alignment, G for three-dimensionally ordered spherical domains remains that of a soft solid, albeit with a much lower modulus than that of the unoriented material (Koppi et al. 1994). [Pg.627]

The first effect of applying a magnetic field to a ferromagnet is the alignment of domains, which is reflected in the spontaneous anisotropy described in section... [Pg.476]

Alignment of domains in mesogenic polymers can be achieved either by polymerizing an aligned monomer or by submitting the mesogenic polymer to a directional deformation in a field of force. [Pg.93]

The efficiency of electric fields for the alignment of domains in block copolymer thin films has been mainly demonstrated in PS-b-PMMA systems where PS forms the matrix. [Pg.39]

The direction of the alignment of magnetic moments within a magnetic domain is related to the axes of the crystal lattice by crystalline electric fields and spin-orbit interaction of transition-metal t5 -ions (24). The dependency is given by the magnetocrystalline anisotropy energy expression for a cubic lattice (33) ... [Pg.189]

Nazem [31] has reported that mesophase pitch exhibits shear-thinning behavior at low shear rates and, essentially, Newtonian behavior at higher shear rates. Since isotropic pitch is Newtonian over a wide range of shear rates, one might postulate that the observed pseudoplasticity of mesophase is due to the alignment of liquid crystalline domains with increasing shear rate. Also, it has been reported that mesophase pitch can exhibit thixotropic behavior [32,33]. It is not clear, however, if this could be attributed to chemical changes within the pitch or, perhaps, to experimental factors. [Pg.129]

Fig. 5. Structure-based alignment of the sequences of the water-soluble Rieske fragment from bovine heart bci complex (ISF), the water-soluble Rieske fragment from spinach b f complex (RFS), and of the Rieske domain of naphthalene dioxygenase (NDO) and of the metal binding loops of rubredoxin (RXN) and transcriptional factor TFIIS (TFI). The numbering of the j3 strands is the same for the ISF and RFS. The metal binding ligands are highlighted the asterisks indicate those residues that are fully conserved between the three Rieske proteins. Fig. 5. Structure-based alignment of the sequences of the water-soluble Rieske fragment from bovine heart bci complex (ISF), the water-soluble Rieske fragment from spinach b f complex (RFS), and of the Rieske domain of naphthalene dioxygenase (NDO) and of the metal binding loops of rubredoxin (RXN) and transcriptional factor TFIIS (TFI). The numbering of the j3 strands is the same for the ISF and RFS. The metal binding ligands are highlighted the asterisks indicate those residues that are fully conserved between the three Rieske proteins.
Fig. 9.18 Comparison of calculated time-domain spectra (NFS) and energy-domain spectra (Mossbauer absorption) for a-, b-, and c-cut single crystals of guanidinium nitroprusside. For the calculations the approximation of complete alignment of 14 parallel to the crystallographic c-axis is used. The polarisation direction of the synchrotron beam is represented by e. (Taken from [48])... Fig. 9.18 Comparison of calculated time-domain spectra (NFS) and energy-domain spectra (Mossbauer absorption) for a-, b-, and c-cut single crystals of guanidinium nitroprusside. For the calculations the approximation of complete alignment of 14 parallel to the crystallographic c-axis is used. The polarisation direction of the synchrotron beam is represented by e. (Taken from [48])...
Fig. 10.4. (Opposite) Alignments of nematode chitinases with the active centre boxed. Identical amino acids are marked with an asterisk ( ) similar amino acids are marked with a dot (.). Conserved cysteine residues in the chitin-binding domain are printed in bold. Gene Bank accession numbers C.eleg. Chit (C. elegans), Q11174 OvL3 Chit (O. volvulus), L42021 AvL3 Chit (A viteae), U14638 B.m. Chit(B. malayi), M73689. Fig. 10.4. (Opposite) Alignments of nematode chitinases with the active centre boxed. Identical amino acids are marked with an asterisk ( ) similar amino acids are marked with a dot (.). Conserved cysteine residues in the chitin-binding domain are printed in bold. Gene Bank accession numbers C.eleg. Chit (C. elegans), Q11174 OvL3 Chit (O. volvulus), L42021 AvL3 Chit (A viteae), U14638 B.m. Chit(B. malayi), M73689.
Fig. 4. Alignment of poly(HASCL) depolymerase C-terminal substrate binding domains. Two types of poly(HASCL) depolymerase C-terminal substrate binding domains (A and B) can be distinguished by amino acid alignment. Amino acids strictly conserved in all depolymerase proteins are indicated... Fig. 4. Alignment of poly(HASCL) depolymerase C-terminal substrate binding domains. Two types of poly(HASCL) depolymerase C-terminal substrate binding domains (A and B) can be distinguished by amino acid alignment. Amino acids strictly conserved in all depolymerase proteins are indicated...
Fig. 4. Multiple sequence alignment of six distinct SH2 domain sequences. The SH2 domain notifiers are given on the left, the bottom line represents the consensus sequence as analyzed from the alignment. Highly conserved sequence positions are marked with capital letters. The sequential position of the major secondary structure elements (helices and sheets) are indicated by boxes... Fig. 4. Multiple sequence alignment of six distinct SH2 domain sequences. The SH2 domain notifiers are given on the left, the bottom line represents the consensus sequence as analyzed from the alignment. Highly conserved sequence positions are marked with capital letters. The sequential position of the major secondary structure elements (helices and sheets) are indicated by boxes...

See other pages where Alignment of domains is mentioned: [Pg.184]    [Pg.331]    [Pg.56]    [Pg.73]    [Pg.336]    [Pg.15]    [Pg.152]    [Pg.31]    [Pg.1096]    [Pg.184]    [Pg.331]    [Pg.56]    [Pg.73]    [Pg.336]    [Pg.15]    [Pg.152]    [Pg.31]    [Pg.1096]    [Pg.519]    [Pg.545]    [Pg.250]    [Pg.309]    [Pg.188]    [Pg.366]    [Pg.381]    [Pg.381]    [Pg.49]    [Pg.221]    [Pg.344]    [Pg.253]    [Pg.394]    [Pg.487]    [Pg.472]    [Pg.796]    [Pg.862]    [Pg.1244]    [Pg.128]    [Pg.162]    [Pg.59]    [Pg.132]    [Pg.205]    [Pg.239]    [Pg.204]    [Pg.508]    [Pg.258]    [Pg.420]    [Pg.54]    [Pg.86]   
See also in sourсe #XX -- [ Pg.366 , Pg.370 ]




SEARCH



Domains alignments

© 2024 chempedia.info