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Out-of-registry interactions

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).
Figure 4 Schematic illustration of intra- and in-registry and out-of-registry interchain interaction present for magnetically ordered [MCp 2][anion]. Reprinted with permission from the copyright owner (in process of obtaining). Figure 4 Schematic illustration of intra- and in-registry and out-of-registry interchain interaction present for magnetically ordered [MCp 2][anion]. Reprinted with permission from the copyright owner (in process of obtaining).
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.

See other pages where Out-of-registry interactions is mentioned: [Pg.446]    [Pg.446]    [Pg.448]    [Pg.446]    [Pg.446]    [Pg.448]    [Pg.117]    [Pg.250]    [Pg.150]    [Pg.134]    [Pg.265]    [Pg.447]    [Pg.454]    [Pg.214]    [Pg.299]    [Pg.447]    [Pg.454]    [Pg.455]    [Pg.134]    [Pg.60]    [Pg.579]   


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