Fermi surface in the hidden-order state of URu2_2Si2_2 under intense pulsed magnetic fields up to 81~T

We present measurements of the resistivity $\rho_{x,x}$ of URu2Si2 high-quality single crystals in pulsed high magnetic fields up to 81~T at a temperature of 1.4~K and up to 60~T at temperatures down to 100~mK. For a field \textbf{H} applied along the magnetic easy-axis \textbf{c}, a strong sample-dependence of the low-temperature resistivity in the hidden-order phase is attributed to a high carrier mobility. The interplay between the magnetic and orbital properties is emphasized by the angle-dependence of the phase diagram, where magnetic transition fields and crossover fields related to the Fermi surface properties follow a 1/$\cos\theta$-law, $\theta$ being the angle between \textbf{H} and \textbf{c}. For $\mathbf{H}\parallel\mathbf{c}$, a crossover defined at a kink of $\rho_{x,x}$, as initially reported in [Shishido et al., Phys. Rev. Lett. \textbf{102}, 156403 (2009)], is found to be strongly sample-dependent: its characteristic field $\mu_0H^*$ varies from $\simeq20$~T in our best sample with a residual resistivity ratio RRR of $225$ to $\simeq25$~T in a sample with a RRR of $90$. A second crossover is defined at the maximum of $\rho_{x,x}$ at the sample-independent characteristic field $\mu_0H_{\rho,max}^{LT}\simeq30$~T. Fourier analyzes of SdH oscillations show that $H_{\rho,max}^{LT}$ coincides with a sudden modification of the Fermi surface, while $H^*$ lies in a regime where the Fermi surface is smoothly modified. For $\mathbf{H}\parallel\mathbf{a}$, i) no phase transition is observed at low temperature and the system remains in the hidden-order phase up to 81~T, ii) quantum oscillations surviving up to 7~K are related to a new and almost-spherical orbit - for the first time observed here - at the frequency $F_\lambda\simeq1400$~T and associated with a low effective mass $m^*_\lambda=(1\pm0.5)\cdot m_0$, and iii) no Fermi surface modification occurs up to 81~T.Comment: 11 pages, 8 figure

High frequency magnetic oscillations of the organic metal θ\theta-(ET)4_4ZnBr4_4(C6_6H4_4Cl2_2) in pulsed magnetic field of up to 81 T

De Haas-van Alphen oscillations of the organic metal $\theta$-(ET)$_4$ZnBr$_4$(C$_6$H$_4$Cl$_2$) are studied in pulsed magnetic fields up to 81 T. The long decay time of the pulse allows determining reliable field-dependent amplitudes of Fourier components with frequencies up to several kiloteslas. The Fourier spectrum is in agreement with the model of a linear chain of coupled orbits. In this model, all the observed frequencies are linear combinations of the frequency linked to the basic orbit $\alpha$ and to the magnetic-breakdown orbit $\beta$.Comment: 6 pages, 4 figure

Collapse of the Mott gap and emergence of a nodal liquid in lightly doped Sr2_2IrO4_4

Superconductivity in underdoped cuprates emerges from an unusual electronic state characterised by nodal quasiparticles and an antinodal pseudogap. The relation between this state and superconductivity is intensely studied but remains controversial. The discrimination between competing theoretical models is hindered by a lack of electronic structure data from related doped Mott insulators. Here we report the doping evolution of the Heisenberg antiferromagnet Sr$_2$IrO$_4$, a close analogue to underdoped cuprates. We demonstrate that metallicity emerges from a rapid collapse of the Mott gap with doping, resulting in lens-like Fermi contours rather than disconnected Fermi arcs as observed in cuprates. Intriguingly though, the emerging electron liquid shows nodal quasiparticles with an antinodal pseudogap and thus bares strong similarities with underdoped cuprates. We conclude that anisotropic pseudogaps are a generic property of two-dimensional doped Mott insulators rather than a unique hallmark of cuprate high-temperature superconductivity

Role of structural dynamics at the receptor G protein interface for signal transduction

GPCRs catalyze GDP/GTP exchange in the α-subunit of heterotrimeric G proteins (Gαßγ) through displacement of the Gα C-terminal α5 helix, which directly connects the interface of the active receptor (R*) to the nucleotide binding pocket of G. Hydrogen-deuterium exchange mass spectrometry and kinetic analysis of R* catalysed G protein activation have suggested that displacement of α5 starts from an intermediate GDP bound complex (R*•GGDP). To elucidate the structural basis of receptor-catalysed displacement of α5, we modelled the structure of R*•GGDP. A flexible docking protocol yielded an intermediate R*•GGDP complex, with a similar overall arrangement as in the X-ray structure of the nucleotide free complex (R*•Gempty), however with the α5 C-terminus (GαCT) forming different polar contacts with R*. Starting molecular dynamics simulations of GαCT bound to R* in the intermediate position, we observe a screw-like motion, which restores the specific interactions of α5 with R* in R*•Gempty. The observed rotation of α5 by 60° is in line with experimental data. Reformation of hydrogen bonds, water expulsion and formation of hydrophobic interactions are driving forces of the α5 displacement. We conclude that the identified interactions between R* and G protein define a structural framework in which the α5 displacement promotes direct transmission of the signal from R* to the GDP binding pocket

Biofouling of crypts of historical and architectural interest at la Plata Cemetery (Argentina)

Cemeteries are part of the cultural heritage of urban communities, containing funerary crypts and monuments of historical and architectural interest. Efforts aimed at the conservation of these structures must target not only the abiotic stresses that cause their destruction, such as light and humidity, but also biofouling by biotic agents. The purpose of this study was to assess the development of biofouling of several historically and architecturally valuable crypts at La Plata Cemetery (Argentina). Samples obtained from the biofilms, lichens, and fungal colonies that had developed on the marble surfaces and cement mortar of these crypts were analyzed by conventional microbiological techniques and by scanning electron microscopy. The lichens were identified as Caloplaca austrocitrina, Lecanora albescens, Xanthoparmelia farinosa and Xanthoria candelaria, the fungi as Aspergillus sp., Penicillium sp., Fusarium sp., Candida sp. and Rhodotorula sp., and the bacteria as Bacillus sp. and Pseudomonas sp. The mechanisms by which these microorganisms cause the aesthetic and biochemical deterioration of the crypts are discussed

The Roles of Transmembrane Domain Helix-III during Rhodopsin Photoactivation

Background: Rhodopsin, the prototypic member of G protein-coupled receptors (GPCRs), undergoes isomerization of 11- cis-retinal to all-trans-retinal upon photoactivation. Although the basic mechanism by which rhodopsin is activated is well understood, the roles of whole transmembrane (TM) helix-III during rhodopsin photoactivation in detail are not completely clear. Principal Findings: We herein use single-cysteine mutagenesis technique to investigate conformational changes in TM helices of rhodopsin upon photoactivation. Specifically, we study changes in accessibility and reactivity of cysteine residues introduced into the TM helix-III of rhodopsin. Twenty-eight single-cysteine mutants of rhodopsin (P107C-R135C) were prepared after substitution of all natural cysteine residues (C140/C167/C185/C222/C264/C316) by alanine. The cysteine mutants were expressed in COS-1 cells and rhodopsin was purified after regeneration with 11-cis-retinal. Cysteine accessibility in these mutants was monitored by reaction with 4, 49-dithiodipyridine (4-PDS) in the dark and after illumination. Most of the mutants except for T108C, G109C, E113C, I133C, and R135C showed no reaction in the dark. Wide variation in reactivity was observed among cysteines at different positions in the sequence 108–135 after photoactivation. In particular, cysteines at position 115, 119, 121, 129, 131, 132, and 135, facing 11-cis-retinal, reacted with 4-PDS faster than neighboring amino acids. The different reaction rates of mutants with 4-PDS after photoactivation suggest that the amino acids in different positions in helix-III are exposed to aqueous environment to varying degrees. Significance: Accessibility data indicate that an aqueous/hydrophobic boundary in helix-III is near G109 and I133. The lack of reactivity in the dark and the accessibility of cysteine after photoactivation indicate an increase of water/4-PDS accessibility for certain cysteine-mutants at Helix-III during formation of Meta II. We conclude that photoactivation resulted in water-accessible at the chromophore-facing residues of Helix-III.National Institutes of Health (U.S.) (grant GM28289)National Eye Institute (Grant Grant EY11716)National Science Foundation (U.S.) (grant EIA-0225609

Free backbone carbonyls mediate rhodopsin activation

Conserved prolines in the transmembrane helices of G-protein-coupled receptors (GPCRs) are often considered to function as hinges that divide the helix into two segments capable of independent motion. Depending on their potential to hydrogen-bond, the free C=O groups associated with these prolines can facilitate conformational flexibility, conformational switching or stabilization of the receptor structure. To address the role of conserved prolines in family A GPCRs through solid-state NMR spectroscopy, we focus on bovine rhodopsin, a GPCR in the visual receptor subfamily. The free backbone C=O groups on helices H5 and H7 stabilize the inactive rhodopsin structure through hydrogen-bonds to residues on adjacent helices. In response to light-induced isomerization of the retinal chromophore, hydrogen-bonding interactions involving these C=O groups are released, thus facilitating repacking of H5 and H7 onto the transmembrane core of the receptor. These results provide insights into the multiple structural and functional roles of prolines in membrane proteins