Ladder-like optical conductivity in the spin-fermion model

In the nested limit of the spin-fermion model for the cuprates, one-dimensional physics in the form of half-filled two-leg ladders emerges. We show that the renormalization group flow of the corresponding ladder is towards the d-Mott phase, a gapped spin-liquid with short-ranged d-wave pairing correlations, and reveals an intermediate SO(5)$\times$SO(3) symmetry. We use the results of the renormalization group in combination with a memory-function approach to calculate the optical conductivity of the spin-fermion model in the high-frequency regime, where processes within the hot spot region dominate the transport. We argue that umklapp processes play a major role. For finite temperatures, we determine the resistivity in the zero-frequency (dc) limit. Our results show an approximate linear temperature dependence of the resistivity and a conductivity that follows a non-universal power law. A comparison to experimental data supports our assumption that the conductivity is dominated by the antinodal contribution above the pseudogap.Comment: 11+2 pages, 8 figure

Motion of a distinguishable impurity in the Bose gas: Arrested expansion without a lattice and impurity snaking

We consider the real time dynamics of an initially localized distinguishable impurity injected into the ground state of the Lieb-Liniger model. Focusing on the case where integrability is preserved, we numerically compute the time evolution of the impurity density operator in regimes far from analytically tractable limits. We find that the injected impurity undergoes a stuttering motion as it moves and expands. For an initially stationary impurity, the interaction-driven formation of a quasibound state with a hole in the background gas leads to arrested expansion -- a period of quasistationary behavior. When the impurity is injected with a finite center of mass momentum, the impurity moves through the background gas in a snaking manner, arising from a quantum Newton's cradle-like scenario where momentum is exchanged back-and-forth between the impurity and the background gas.Comment: v1: 13 pages, 10 figures; v2: 14 pages, 13 figures and change of titl

Umklapp scattering as the origin of TT-linear resistivity in the normal state of high-TcT_c cuprate superconductors

The high-temperature normal state of the unconventional cuprate superconductors has resistivity linear in temperature $T$, which persists to values well beyond the Mott-Ioffe-Regel upper bound. At low-temperature, within the pseudogap phase, the resistivity is instead quadratic in $T$, as would be expected from Fermi liquid theory. Developing an understanding of these normal phases of the cuprates is crucial to explain the unconventional superconductivity. We present a simple explanation for this behavior, in terms of umklapp scattering of electrons. This fits within the general picture emerging from functional renormalization group calculations that spurred the Yang-Rice-Zhang ansatz: umklapp scattering is at the heart of the behavior in the normal phase.Comment: v1 6+1 pages, 4 figures; v2 6+2 pages, 4 figures; v3 6 + 2.5 pages, 5 figure

Folding of a single domain protein entering the endoplasmic reticulum precedes disulfide formation

The relationship between protein synthesis, folding and disulfide formation within the endoplasmic reticulum (ER) is poorly understood. Previous studies have suggested pre-existing disulfide links are absolutely required to allow protein folding and, conversely, that protein folding occurs prior to disulfide formation. To address the question of what happens first within the ER; that is, protein folding or disulfide formation, we studied folding events at the early stages of polypeptide chain translocation into the mammalian ER using stalled translation intermediates. Our results demonstrate that polypeptide folding can occur without complete domain translocation. Protein disulfide isomerase (PDI) interacts with these early intermediates, but disulfide formation does not occur unless the entire sequence of the protein domain is translocated. This is the first evidence that folding of the polypeptide chain precedes disulfide formation within a cellular context and highlights key differences between protein folding in the ER and refolding of purified proteins

Prethermalization and thermalization in models with weak integrability breaking

We study the effects of integrability breaking perturbations on the non-equilibrium evolution of many-particle quantum systems. We focus on a class of spinless fermion models with weak interactions. We employ equation of motion techniques that can be viewed as generalizations of quantum Boltzmann equations. We benchmark our method against time dependent density matrix renormalization group computations and find it to be very accurate as long as interactions are weak. For small integrability breaking, we observe robust prethermalization plateaux for local observables on all accessible time scales. Increasing the strength of the integrability breaking term induces a "drift" away from the prethermalization plateaux towards thermal behaviour. We identify a time scale characterizing this cross-over.Comment: 9 pages, 4 figure

"Quasi-particle breakdown" in the quasi-one-dimensional Ising ferromagnet CoNb2_2O6_6

We present experimental and theoretical evidence that an interesting quantum many-body effect -- quasi-particle breakdown -- occurs in the quasi-one-dimensional spin-1/2 Ising-like ferromagnet CoNb$_2$O$_6$ in its paramagnetic phase at high transverse field as a result of explicit breaking of spin inversion symmetry. We propose a quantum spin Hamiltonian capturing the essential one-dimensional physics of CoNb$_2$O$_6$ and determine the exchange parameters of this model by fitting the calculated single particle dispersion to the one observed experimentally in applied transverse magnetic fields. We present high-resolution inelastic neutron scattering measurements of the single particle dispersion which observe "anomalous broadening" effects over a narrow energy range at intermediate energies. We propose that this effect originates from the decay of the one particle mode into two-particle states. This decay arises from (i) a finite overlap between the one-particle dispersion and the two-particle continuum in a narrow energy-momentum range and (ii) a small misalignment of the applied field away from the direction perpendicular to the Ising axis in the experiments, which allows for non-zero matrix elements for decay by breaking the $\mathbb{Z}_2$ spin inversion symmetry of the Hamiltonian.Comment: v1: 15 pages, 10 figures. v2: 16 pages, 10 figures, minor changes, as accepted to PR

Mechanisms of disulfide bond formation in nascent polypeptides entering the secretory pathway

Disulfide bonds are an abundant feature of proteins across all domains of life that are important for structure, stability, and function. In eukaryotic cells, a major site of disulfide bond formation is the endoplasmic reticulum (ER). How cysteines correctly pair during polypeptide folding to form the native disulfide bond pattern is a complex problem that is not fully understood. In this paper, the evidence for different folding mechanisms involved in ER-localised disulfide bond formation is reviewed with emphasis on events that occur during ER entry. Disulfide formation in nascent polypeptides is discussed with focus on (i) its mechanistic relationship with conformational folding, (ii) evidence for its occurrence at the co-translational stage during ER entry, and (iii) the role of protein disulfide isomerase (PDI) family members. This review highlights the complex array of cellular processes that influence disulfide bond formation and identifies key questions that need to be addressed to further understand this fundamental process

Signatures of rare states and thermalization in a theory with confinement

There is a dichotomy in the nonequilibrium dynamics of quantum many-body systems. In the presence of integrability, expectation values of local operators equilibrate to values described by a generalized Gibbs ensemble, which retains extensive memory about the initial state of the system. On the other hand, in generic systems such expectation values relax to stationary values described by the thermal ensemble, fixed solely by the energy of the state. At the heart of understanding, this dichotomy is the eigenstate thermalization hypothesis (ETH): individual eigenstates in nonintegrable systems are thermal, in the sense that expectation values agree with the thermal prediction at a temperature set by the energy of the eigenstate. In systems where ETH is violated, thermalization can be avoided. Thus, establishing the range of validity of ETH is crucial in understanding whether a given quantum system thermalizes. Here, we study a simple model with confinement, the quantum Ising chain with a longitudinal field, in which ETH is violated. Despite an absence of integrability, there exist rare (nonthermal) states that persist far into the spectrum. These arise as a direct consequence of confinement: pairs of particles are confined, forming new “meson” excitations whose energy can be extensive in the system size. We show that such states are nonthermal in both the continuum and in the low-energy spectrum of the corresponding lattice model. We highlight that the presence of such states within the spectrum has important consequences, with certain quenches leading to an absence of thermalization and local observables evolving anomalously

Protein secondary structure determines the temporal relationship between folding and disulfide formation

How and when disulfides bonds form in proteins relative to the stage of their folding is a fundamental question in cell biology. Two models describe this relationship, the folded precursor model, in which a nascent structure forms before disulfides do and the quasi-stochastic model where disulfides form prior to folding. Here we investigated oxidative folding of three structurally diverse substrates, β2-microglobulin (β2M), prolactin, and the disintegrin domain of ADAM metallopeptidase domain 10 (ADAM10), to understand how these mechanisms apply in a cellular context. We used a eukaryotic cell-free translation system in which we could identify disulfide isomers in stalled translation intermediates to characterize (i) the timing of disulfide formation relative to translocation into the endoplasmic reticulum and (ii) the presence of non-native disulfides. Our results indicate that in a domain lacking secondary structure, disulfides form before conformational folding through a process prone to non-native disulfide formation, whereas in proteins with defined secondary structure, native disulfide formation occurs after partial folding. These findings reveal that the nascent protein structure promotes correct disulfide formation during co-translational folding