7 research outputs found
Disentangling Cooper-pair formation above Tc from the pseudogap state in the cuprates
The discovery of the pseudogap in the cuprates created significant excitement
amongst physicists as it was believed to be a signature of pairing, in some
cases well above the room temperature. In this "pre-formed pairs" scenario, the
formation of pairs without quantum phase rigidity occurs below T*. These pairs
condense and develop phase coherence only below Tc. In contrast, several recent
experiments reported that the pseudogap and superconducting states are
characterized by two different energy scales, pointing to a scenario, where the
two compete. However a number of transport, magnetic, thermodynamic and
tunneling spectroscopy experiments consistently detect a signature of
phase-fluctuating superconductivity above leaving open the question of whether
the pseudogap is caused by pair formation or not. Here we report the discovery
of a spectroscopic signature of pair formation and demonstrate that in a region
of the phase diagram commonly referred to as the "pseudogap", two distinct
states coexist: one that persists to an intermediate temperature Tpair and a
second that extends up to T*. The first state is characterized by a doping
independent scaling behavior and is due to pairing above Tc, but significantly
below T*. The second state is the "proper" pseudogap - characterized by a
"checker board" pattern in STM images, the absence of pair formation, and is
likely linked to Mott physics of pristine CuO2 planes. Tpair has a universal
value around 130-150K even for materials with very different Tc, likely setting
limit on highest, attainable Tc in cuprates. The observed universal scaling
behavior with respect to Tpair indicates a breakdown of the classical picture
of phase fluctuations in the cuprates.Comment: 9 pages, 4 figure
Critical change in the Fermi surface of iron arsenic superconductors at the onset of superconductivity
The phase diagram of a correlated material is the result of a complex
interplay between several degrees of freedom, providing a map of the material's
behavior. One can understand (and ultimately control) the material's ground
state by associating features and regions of the phase diagram, with specific
physical events or underlying quantum mechanical properties. The phase diagram
of the newly discovered iron arsenic high temperature superconductors is
particularly rich and interesting. In the AE(Fe1-xTx)2As2 class (AE being Ca,
Sr, Ba, T being transition metals), the simultaneous structural/magnetic phase
transition that occurs at elevated temperature in the undoped material, splits
and is suppressed by carrier doping, the suppression being complete around
optimal doping. A dome of superconductivity exists with apparent equal ease in
the orthorhombic / antiferromagnetic (AFM) state as well as in the tetragonal
state with no long range magnetic order. The question then is what determines
the critical doping at which superconductivity emerges, if the AFM order is
fully suppressed only at higher doping values. Here we report evidence from
angle resolved photoemission spectroscopy (ARPES) that critical changes in the
Fermi surface (FS) occur at the doping level that marks the onset of
superconductivity. The presence of the AFM order leads to a reconstruction of
the electronic structure, most significantly the appearance of the small hole
pockets at the Fermi level. These hole pockets vanish, i. e. undergo a Lifshitz
transition, at the onset of superconductivity. Superconductivity and magnetism
are competing states in the iron arsenic superconductors. In the presence of
the hole pockets superconductivity is fully suppressed, while in their absence
the two states can coexist.Comment: Updated version accepted in Nature Physic
Structural Impact of the E113Q Counterion Mutation on the Activation and Deactivation Pathways of the G Protein-coupled Receptor Rhodopsin
Disruption of an interhelical salt bridge between the retinal protonated Schiff base linked to H7 and Glu113 on H3 is one of the decisive steps during activation of rhodopsin. Using previously established stabilization strategies, we engineered a stabilized E113Q counterion mutant that converted rhodopsin to a UV-absorbing photoreceptor with deprotonated Schiff base and allowed reconstitution into native-like lipid membranes. Fourier-transform infrared difference spectroscopy reveals a deprotonated Schiff base in the photoproducts of the mutant up to the active state Meta II, the absence of the classical pH-dependent Meta I/Meta II conformational equilibrium in favor of Meta II, and an anticipation of active state features under conditions that stabilize inactive photoproduct states in wildtype rhodopsin. Glu181 on extracellular loop 2, is found to be unable to maintain a counterion function to the Schiff base on the activation pathway of rhodopsin in the absence of the primary counterion, Glu113. The Schiff base becomes protonated in the transition to Meta III. This protonation is, however, not associated with a deactivation of the receptor, in contrast to wildtype rhodopsin. Glu181 is suggested to be the counterion in the Meta III state of the mutant and appears to be capable of stabilizing a protonated Schiff base in Meta III, but not of constraining the receptor in an inactive conformation
Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser
G-protein-coupled receptors (GPCRs) signal primarily through G proteins or arrestins. Arrestin binding to GPCRs blocks G protein interaction and redirects signalling to numerous G-protein-independent pathways. Here we report the crystal structure of a constitutively active form of human rhodopsin bound to a pre-activated form of the mouse visual arrestin, determined by serial femtosecond X-ray laser crystallography. Together with extensive biochemical and mutagenesis data, the structure reveals an overall architecture of the rhodopsin–arrestin assembly in which rhodopsin uses distinct structural elements, including transmembrane helix 7 and helix 8, to recruit arrestin. Correspondingly, arrestin adopts the pre-activated conformation, with a ~20° rotation between the amino and carboxy domains, which opens up a cleft in arrestin to accommodate a short helix formed by the second intracellular loop of rhodopsin. This structure provides a basis for understanding GPCR-mediated arrestin-biased signalling and demonstrates the power of X-ray lasers for advancing the frontiers of structural biology