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Out-of-registry chains

Fig. 8-4. The solid state ID-DADA structure of the bulk ferromagnet [FeCpJ] [TCNE] . Inregistry chains (I—II) and out-of-registry chains (II —III), as well as selected interatomic distances are shown (reprinted with permission from ref [28], copyright 1987 American Chemical Society). Fig. 8-4. The solid state ID-DADA structure of the bulk ferromagnet [FeCpJ] [TCNE] . Inregistry chains (I—II) and out-of-registry chains (II —III), as well as selected interatomic distances are shown (reprinted with permission from ref [28], copyright 1987 American Chemical Society).
Again, the same 1 D-D ADA structure was found for the hexacyanobutadienide CT complex, as illustrated in Fig. 8-6. This material also displays in-registry and out-of-registry interactions between chains, as is the case for [FeCpf]" [TCNE] . Furthermore, it shows dominant ferromagnetic interactions, as indicated by the Curie-Weiss constant 0 -)- 35 K [29]. [Pg.444]

Fig. 8-8. The solid state structure of the 2 1 CT complex [FeCp ] 2 [TCNQF4] showing the out-of-registry interactions between chains of the DADDAD type (reprinted with permission from ref. [32], copyright 1989 American Chemical Society). Fig. 8-8. The solid state structure of the 2 1 CT complex [FeCp ] 2 [TCNQF4] showing the out-of-registry interactions between chains of the DADDAD type (reprinted with permission from ref. [32], copyright 1989 American Chemical Society).
Fig. 6. Organization of apolipoprotein molecules in discoidal HDL particles. (A) Double belt model for apo A1 structure at the edge of discoidal HDL complex. Two ring-shaped molecules of apo A1 are stacked on top of each other with both molecules in an anti-parallel orientation, allowing the helix registry to maximize intermolecular salt-bridge interactions. Only the charged residues at selected positions are explicitly displayed. (B) Model of apo E in discoidal HDL complex depicting the locations of engineered tryptophan residues on helix 4. Fluorescence from these amino acids was monitored to determine helix orientation. Two out of a total of about four mole-cules/particles of apo E are depicted in which the helical axes are oriented perpendicular to the PL acyl chains. Fig. 6. Organization of apolipoprotein molecules in discoidal HDL particles. (A) Double belt model for apo A1 structure at the edge of discoidal HDL complex. Two ring-shaped molecules of apo A1 are stacked on top of each other with both molecules in an anti-parallel orientation, allowing the helix registry to maximize intermolecular salt-bridge interactions. Only the charged residues at selected positions are explicitly displayed. (B) Model of apo E in discoidal HDL complex depicting the locations of engineered tryptophan residues on helix 4. Fluorescence from these amino acids was monitored to determine helix orientation. Two out of a total of about four mole-cules/particles of apo E are depicted in which the helical axes are oriented perpendicular to the PL acyl chains.
I been established to serve as a registry of convicted offenders. When a DNA sample is obtained from a crime scene, the sample is subjected to cleavage with restriction endonucleases to cut out fragments containing the STR loci, the fragments are amplified using the polymerase chain reaction, and the sequences of the fragments are determined. [Pg.1119]


See other pages where Out-of-registry chains is mentioned: [Pg.117]    [Pg.117]    [Pg.122]    [Pg.446]    [Pg.447]    [Pg.329]    [Pg.446]    [Pg.447]    [Pg.448]    [Pg.455]    [Pg.329]    [Pg.60]    [Pg.1184]    [Pg.1119]    [Pg.477]    [Pg.1186]    [Pg.1206]    [Pg.1119]    [Pg.1186]    [Pg.1010]    [Pg.1146]    [Pg.77]   
See also in sourсe #XX -- [ Pg.443 ]

See also in sourсe #XX -- [ Pg.443 ]




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