Ginzburg-Landau theory of phase transitions in quasi-one-dimensional systems

A wide range of quasi-one-dimensional materials, consisting of weakly coupled chains, undergo three-dimensional phase transitions that can be described by a complex order parameter. A Ginzburg-Landau theory is derived for such a transition. It is shown that intrachain fluctuations in the order parameter play a crucial role and must be treated exactly. The effect of these fluctuations is determined by a single dimensionless parameter. The three-dimensional transition temperature, the associated specific heat jump, coherence lengths, and width of the critical region, are computed assuming that the single chain Ginzburg-Landau coefficients are independent of temperature. The width of the critical region, estimated from the Ginzburg criterion, is virtually parameter independent, being about 5-8 per cent of the transition temperature. To appear in {\it Physical Review B,} March 1, 1995.Comment: 15 pages, RevTeX, 5 figures in uuencoded compressed tar file

Impurity-induced transition and impurity-enhanced thermopower in the thermoelectric oxide NaCo_{2-x}Cu_x$O_4

Various physical quantities are measured and analysed for the Cu-substituted thermoelectric oxide NaCo_{2-x}Cu_xO_4. As was previously known, the substituted Cu enhances the thermoelectric power, while it does not increase the resistivity significantly. The susceptibility and the electron specific-heat are substantially decreased with increasing x, which implies that the substituted Cu decreases the effective-mass enhancement. Through a quantitative comparison with the heavy fermion compounds and the valence fluctuation systems, we have found that the Cu substitution effectively increases the coupling between the conduction electron and the magnetic fluctuation. The Cu substitution induces a phase transition at 22 K that is very similar to a spin-density-wave transition.Comment: 8 pages, 7 figures, submitted to Phys. Rev.

Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking

The techniques of phage-displayed homolog shotgun scanning, oligomer complementation, NMR secondary structure analysis, and computational docking provide a complementary suite of tools for dissecting protein–protein interactions. Focusing these tools on the interaction between the catalytic sub-unit of protein kinase A (PKAcat) and caveolin-1 scaffolding domain (CSD) reveals the first structural model for the interaction. Homolog shotgun scanning varied each CSD residue as either a wild-type or a homologous amino acid. Wild-type to homolog ratios from 116 different homologous CSD variants identified side-chain functional groups responsible for precise contacts with PKAcat. Structural analysis by NMR assigned an α-helical conformation to the central residues 84– 97 of CSD. The extensive mutagenesis data and NMR secondary structure information provided constraints for developing a model for the PKAcat–CSD interaction. Addition of synthetic CSD to phage-displayed CSD resulted in oligomer complementation, or enhanced binding to PKAcat. Together with previous experiments examining the interaction between CSD and endothelial nitric oxide synthase (eNOS), the results suggest a general oligomerization-dependent enhancement of binding between signal transducing enzymes and caveolin-1

Exploring the interaction between the protein kinase A catalytic subunit and caveolin-1 scaffolding domain with shotgun scanning, oligomer complementation, NMR, and docking.

The techniques of phage-displayed homolog shotgun scanning, oligomer complementation, NMR secondary structure analysis, and computational docking provide a complementary suite of tools for dissecting protein-protein interactions. Focusing these tools on the interaction between the catalytic sub-unit of protein kinase A (PKAcat) and caveolin-1 scaffolding domain (CSD) reveals the first structural model for the interaction. Homolog shotgun scanning varied each CSD residue as either a wild-type or a homologous amino acid. Wild-type to homolog ratios from 116 different homologous CSD variants identified side-chain functional groups responsible for precise contacts with PKAcat. Structural analysis by NMR assigned an alpha-helical conformation to the central residues 84- 97 of CSD. The extensive mutagenesis data and NMR secondary structure information provided constraints for developing a model for the PKAcat-CSD interaction. Addition of synthetic CSD to phage-displayed CSD resulted in oligomer complementation, or enhanced binding to PKAcat. Together with previous experiments examining the interaction between CSD and endothelial nitric oxide synthase (eNOS), the results suggest a general oligomerization-dependent enhancement of binding between signal transducing enzymes and caveolin-1

Electrical characteristics of carbon nanotube devices prepared with single oxidative point defects

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