580 research outputs found

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

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    We present measurements of the resistivity ρx,x\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/cosθ\cos\theta-law, θ\theta being the angle between \textbf{H} and \textbf{c}. For Hc\mathbf{H}\parallel\mathbf{c}, a crossover defined at a kink of ρx,x\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 μ0H\mu_0H^* varies from 20\simeq20~T in our best sample with a residual resistivity ratio RRR of 225225 to 25\simeq25~T in a sample with a RRR of 9090. A second crossover is defined at the maximum of ρx,x\rho_{x,x} at the sample-independent characteristic field μ0Hρ,maxLT30\mu_0H_{\rho,max}^{LT}\simeq30~T. Fourier analyzes of SdH oscillations show that Hρ,maxLTH_{\rho,max}^{LT} coincides with a sudden modification of the Fermi surface, while HH^* lies in a regime where the Fermi surface is smoothly modified. For Ha\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 Fλ1400F_\lambda\simeq1400~T and associated with a low effective mass mλ=(1±0.5)m0m^*_\lambda=(1\pm0.5)\cdot m_0, and iii) no Fermi surface modification occurs up to 81~T.Comment: 11 pages, 8 figure

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

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    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 Sr2_2IrO4_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

    Free backbone carbonyls mediate rhodopsin activation

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    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

    Helix movement is coupled to displacement of the second extracellular loop in rhodopsin activation

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    The second extracellular loop (EL2) of rhodopsin forms a cap over the binding site of its photoreactive 11-cis retinylidene chromophore. A crucial question has been whether EL2 forms a reversible gate that opens upon activation or acts as a rigid barrier. Distance measurements using solid-state 13C NMR spectroscopy between the retinal chromophore and the β4 strand of EL2 show that the loop is displaced from the retinal binding site upon activation, and there is a rearrangement in the hydrogen-bonding networks connecting EL2 with the extracellular ends of transmembrane helices H4, H5 and H6. NMR measurements further reveal that structural changes in EL2 are coupled to the motion of helix H5 and breaking of the ionic lock that regulates activation. These results provide a comprehensive view of how retinal isomerization triggers helix motion and activation in this prototypical G protein-coupled receptor. © 2009 Nature America, Inc. All rights reserved

    Phytochrome Mediated Responses in Agrobacterium fabrum: Growth, Motility and Plant Infection

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    The soil bacterium and plant pathogen Agrobacterium fabrum C58 has two phytochrome photoreceptors, Agp1 and Agp2. We found that plant infection and tumor induction by A. fabrum is down-regulated by light and that phytochrome knockout mutants of A. fabrum have diminished infection rates. The regulation pattern of infection matches with that of bacterial conjugation reported earlier, suggesting similar regulatory mechanisms. In the regulation of conjugation and plant infection, phytochromes are active in darkness. This is a major difference to plant phytochromes, which are typically active after irradiation. We also found that propagation and motility were affected in agp1− and agp2− knockout mutants, although propagation was not always affected by light. The regulatory patterns can partially but not completely be explained by modulated histidine kinase activities of Agp1 and Agp2. In a mass spectrometry-based proteomic study, 24 proteins were different between light and dark grown A. fabrum, whereas 382 proteins differed between wild type and phytochrome knockout mutants, pointing again to light independent roles of Agp1 and Agp2

    Structures of ribosome-bound initiation factor 2 reveal mechanism of subunit association

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    Throughout the four phases of protein biosynthesis—initiation, elongation, termination, and recycling—the ribosome is controlled and regulated by at least one specified translational guanosine triphosphatase (trGTPase). Although the structural basis for trGTPase interaction with the ribosome has been solved for the last three steps of translation, the high-resolution structure for the key initiation trGTPase, initiation factor 2 (IF2), complexed with the ribosome, remains elusive. We determine the structure of IF2 complexed with a nonhydrolyzable guanosine triphosphate analog and initiator fMet-tRNAiMet in the context of the Escherichia coli ribosome to 3.7-Å resolution using cryo-electron microscopy. The structural analysis reveals previously unseen intrinsic conformational modes of the 70S initiation complex, establishing the mutual interplay of IF2 and initator transfer RNA (tRNA) with the ribsosome and providing the structural foundation for a mechanistic understanding of the final steps of translation initiation

    Molecular architecture of the ribosome-bound Hepatitis C Virus internal ribosomal entry site RNA

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    Internal ribosomal entry sites (IRESs) are structured cis‐acting RNAs that drive an alternative, cap‐independent translation initiation pathway. They are used by many viruses to hijack the translational machinery of the host cell. IRESs facilitate translation initiation by recruiting and actively manipulating the eukaryotic ribosome using only a subset of canonical initiation factor and IRES transacting factors. Here we present cryo‐EM reconstructions of the ribosome 80S‐ and 40S‐bound Hepatitis C Virus (HCV) IRES. The presence of four subpopulations for the 80S•HCV IRES complex reveals dynamic conformational modes of the complex. At a global resolution of 3.9 Å for the most stable complex, a derived atomic model reveals a complex fold of the IRES RNA and molecular details of its interaction with the ribosome. The comparison of obtained structures explains how a modular architecture facilitates mRNA loading and tRNA binding to the P‐site. This information provides the structural foundation for understanding the mechanism of HCV IRES RNA‐driven translation initiation

    Cryo-EM captures early ribosome assembly in action

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    Ribosome biogenesis is a fundamental multi-step cellular process in all domains of life that involves the production, processing, folding, and modification of ribosomal RNAs (rRNAs) and ribosomal proteins. To obtain insights into the still unexplored early assembly phase of the bacterial 50S subunit, we exploited a minimal in vitro reconstitution system using purified ribosomal components and scalable reaction conditions. Time-limited assembly assays combined with cryo-EM analysis visualizes the structurally complex assembly pathway starting with a particle consisting of ordered density for only ~500 nucleotides of 23S rRNA domain I and three ribosomal proteins. In addition, our structural analysis reveals that early 50S assembly occurs in a domain-wise fashion, while late 50S assembly proceeds incrementally. Furthermore, we find that both ribosomal proteins and folded rRNA helices, occupying surface exposed regions on pre-50S particles, induce, or stabilize rRNA folds within adjacent regions, thereby creating cooperativity
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