Unconventional Hall effect near charge neutrality point in a two-dimensional electron-hole system

The transport properties of the two-dimensional system in HgTe-based quantum wells containing simultaneously electrons and holes of low densities are examined. The Hall resistance, as a function of perpendicular magnetic field, reveals an unconventional behavior, different from the classical N-shaped dependence typical for bipolar systems with electron-hole asymmetry. The quantum features of magnetotransport are explained by means of numerical calculation of the Landau level spectrum based on the Kane Hamiltonian. The origin of the quantum Hall plateau {\sigma}xy = 0 near the charge neutrality point is attributed to special features of Landau quantization in our system.Comment: 8 pages, 7 figure

On the spectrum of facet crystallization waves at the smooth 4He crystal surface

The wavelike processes of crystallization and melting or crystallization waves are well known to exist at the 4He crystal surface in the rough state. Much less is known about crystallization waves for the 4He crystal surface in the smooth well-faceted state below the roughening transition temperature. To meet the lack, we analyze here the spectrum of facet crystallization waves and its dependence upon the wavelength, perturbation amplitude, and the number of possible facet steps distributed somehow over the wavelength. All the distinctive features of facet crystallization waves from conventional waves at the rough surface result from a nonanalytic cusplike behavior in the angle dependence for the surface tension of smooth crystal facets.Comment: 7 pages, 3 figures, 1 tabl

Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3ζ

AbstractSerine residues phosphorylated by protein kinase A (PKA) in the shortest isoform of human tau protein (τ3) were sequentially replaced by alanine and interaction of phosphorylated τ3 and its mutants with 14-3-3 was investigated. Mutation S156A slightly decreased interaction of phosphorylated τ3 with 14-3-3. Double mutations S156A/S267A and especially S156A/S235A, strongly inhibited interaction of phosphorylated τ3 with 14-3-3. Thus, two sites located in the Pro-rich region and in the pseudo repeats of τ3 are involved in phosphorylation-dependent interaction of τ3 with 14-3-3. The state of τ3 phosphorylation affects the mode of 14-3-3 binding and by this means might modify tau filament formation.Structured summaryMINT-7233358, MINT-7233372, MINT-7233384: 14-3-3 zeta (uniprotkb:P63104) and Tau 3 (uniprotkb:P10636-3) bind (MI:0407) by molecular sieving (MI:0071)MINT-7233323, MINT-7233334, MINT-7233346: Tau 3 (uniprotkb:P10636-3) and 14-3-3 zeta (uniprotkb:P63104) bind (MI:0407) by crosslinking studies (MI:0030)MINT-7233285, MINT-7233297, MINT-7233310: 14-3-3 zeta (uniprotkb:P63104) and Tau 3 (uniprotkb:P10636-3) bind (MI:0407) by comigration in non-denaturing gel electrophoresis (MI:0404