Making ARPES Measurements on Corrugated Monolayer Crystals: Suspended Exfoliated Single-Crystal Graphene

Free-standing exfoliated monolayer graphene is an ultra-thin flexible membrane, which exhibits out of plane deformation or corrugation. In this paper, a technique is described to measure the band structure of such free-standing graphene by angle-resolved photoemission. Our results show that photoelectron coherence is limited by the crystal corrugation. However, by combining surface morphology measurements of the graphene roughness with angle-resolved photoemission, energy dependent quasiparticle lifetime and bandstructure measurements can be extracted. Our measurements rely on our development of an analytical formulation for relating the crystal corrugation to the photoemission linewidth. Our ARPES measurements show that, despite significant deviation from planarity of the crystal, the electronic structure of exfoliated suspended graphene is nearly that of ideal, undoped graphene; we measure the Dirac point to be within 25 meV of $E_F$ . Further, we show that suspended graphene behaves as a marginal Fermi-liquid, with a quasiparticle lifetime which scales as $(E - E_F)^{-1}$; comparison with other graphene and graphite data is discussed

Cryogenic characterisation and modelling of commercial SiC MOSFETs

Two commercial 1.2 kV SiC MOSFETs have been extensively characterised from 30 to 320 K. The temperature dependence of their I/V characteristics, threshold voltage, and breakdown voltage has been examined and are presented in this paper. Overall, the measured characteristics of both devices demonstrate very similar temperature dependencies and it is shown that below ~100 K any further decrease in temperature has little effect on any of the tested characteristics. Increasing temperature beyond 100 K results in a decrease in drain current for a given drain-source and gate-source voltage, a decrease in threshold voltage, and an increase in breakdown voltage. Successful attempts have been made to model the results of these tests by applying theories found in the literature

Functional oxide as an extreme high-k dielectric towards 4H-SiC MOSFET incorporation

MOS Capacitors are demonstrated on 4H-SiC using an octahedral ABO3 ferroic thin-film as a dielectric prepared on several buffer layers. Five samples were prepared: ABO3 on SiC, ABO3 on SiC with a SiO2 buffer (10 nm and 40 nm) and ABO3 on SiC with an Al2O3 buffer (10nm and 40 nm). Depending on the buffer material the oxide forms in either the pyrochlore or perovskite phase. A better lattice match with the Al2O3 buffer yields a perovskite phase with internal switchable dipoles. Hysteresis polarization-voltage loops show an oxide capacitance of ~ 0.2 μF/cm2 in the accumulation region indicating a dielectric constant of ~120

Extraordinary magnetic response of an anisotropic 2D antiferromagnet via site-dilution

A prominent character of two-dimensional magnetic systems is the enhanced spin fluctuations, which however reduce the ordering temperature. Here we report that a magnetic field of only one-thousandth of the Heisenberg superexchange interaction can induce a crossover, which for practical purposes is the effective ordering transition, at temperatures about 6 times of the Neel transition in a site-diluted two-dimensional anisotropic quantum antiferromagnet. Such a strong magnetic response is enabled because the system directly enters the antiferromagnetically ordered state from the isotropic disordered state skipping the intermediate anisotropic stage. The underlying mechanism is achieved on a pseudospin-half square lattice realized in the [(SrIrO3)1/(SrTiO3)2] superlattice thin film that is designed to linearly couple the staggered magnetization to external magnetic fields by virtue of the rotational symmetry-preserving Dzyaloshinskii Moriya interaction. Our model analysis shows that the skipping of the anisotropic regime despite the finite anisotropy is due to the enhanced isotropic fluctuations under moderate dilution

Quantifying particle size and turbulent scale dependence of dust uplift in the Sahara using aircraft measurements

The first size-resolved airborne measurements of dust fluxes and the first dust flux measurements from the central Sahara are presented and compared with a parameterization by Kok (2011a). High-frequency measurements of dust size distribution were obtained from 0.16 to 300 µm diameter, and eddy covariance fluxes were derived. This is more than an order of magnitude larger size range than previous flux estimates. Links to surface emission are provided by analysis of particle drift velocities. Number flux is described by a −2 power law between 1 and 144 µm diameter, significantly larger than the 12 µm upper limit suggested by Kok (2011a). For small particles, the deviation from a power law varies with terrain type and the large size cutoff is correlated with atmospheric vertical turbulent kinetic energy, suggesting control by vertical transport rather than emission processes. The measured mass flux mode is in the range 30–100 µm. The turbulent scales important for dust flux are from 0.1 km to 1–10 km. The upper scale increases during the morning as boundary layer depth and eddy size increase. All locations where large dust fluxes were measured had large topographical variations. These features are often linked with highly erodible surface features, such as wadis or dunes. We also hypothesize that upslope flow and flow separation over such features enhance the dust flux by transporting large particles out of the saltation layer. The tendency to locate surface flux measurements in open, flat terrain means these favored dust sources have been neglected in previous studies

Cryogenic characterization of commercial SiC Power MOSFETs

The cryogenic performance of two commercially available SiC power MOSFETs are presented in this work. The devices are characterised in static and dynamic tests at 10 K intervals from 20-320 K. Static current-voltage characterisation indicates that at low temperatures threshold voltage, turn-on voltage, on-state resistance, transconductance, and the body diode turn-on voltage all increase while saturation current decreases. Dynamic, 60 V, 3A switching tests within the cryogenic chamber are also reported and the trends of switching speed, losses, and total power losses, which rise at low temperature, are presented. Overall, both MOSFETs are fully operable down to 30 K with both positive and negative changes in behaviour

Direct and Absolute Quantification of over 1800 Yeast Proteins via Selected Reaction Monitoring

Defining intracellular protein concentration is critical in molecular systems biology. Although strategies for determining relative protein changes are available, defining robust absolute values in copies per cell has proven significantly more challenging. Here we present a reference data set quantifying over 1800 Saccharomyces cerevisiae proteins by direct means using protein-specific stable-isotope labeled internal standards and selected reaction monitoring (SRM) mass spectrometry, far exceeding any previous study. This was achieved by careful design of over 100 QconCAT recombinant proteins as standards, defining 1167 proteins in terms of copies per cell and upper limits on a further 668, with robust CVs routinely less than 20%. The selected reaction monitoring-derived proteome is compared with existing quantitative data sets, highlighting the disparities between methodologies. Coupled with a quantification of the transcriptome by RNA-seq taken from the same cells, these data support revised estimates of several fundamental molecular parameters: a total protein count of ∼100 million molecules-per-cell, a median of ∼1000 proteins-per-transcript, and a linear model of protein translation explaining 70% of the variance in translation rate. This work contributes a “gold-standard” reference yeast proteome (including 532 values based on high quality, dual peptide quantification) that can be widely used in systems models and for other comparative studies. Reliable and accurate quantification of the proteins present in a cell or tissue remains a major challenge for post-genome scientists. Proteins are the primary functional molecules in biological systems and knowledge of their abundance and dynamics is an important prerequisite to a complete understanding of natural physiological processes, or dysfunction in disease. Accordingly, much effort has been spent in the development of reliable, accurate and sensitive techniques to quantify the cellular proteome, the complement of proteins expressed at a given time under defined conditions (1). Moreover, the ability to model a biological system and thus characterize it in kinetic terms, requires that protein concentrations be defined in absolute numbers (2, 3). Given the high demand for accurate quantitative proteome data sets, there has been a continual drive to develop methodology to accomplish this, typically using mass spectrometry (MS) as the analytical platform. Many recent studies have highlighted the capabilities of MS to provide good coverage of the proteome at high sensitivity often using yeast as a demonstrator system (4⇓⇓⇓⇓⇓–10), suggesting that quantitative proteomics has now “come of age” (1). However, given that MS is not inherently quantitative, most of the approaches produce relative quantitation and do not typically measure the absolute concentrations of individual molecular species by direct means. For the yeast proteome, epitope tagging studies using green fluorescent protein or tandem affinity purification tags provides an alternative to MS. Here, collections of modified strains are generated that incorporate a detectable, and therefore quantifiable, tag that supports immunoblotting or fluorescence techniques (11, 12). However, such strategies for copies per cell (cpc) quantification rely on genetic manipulation of the host organism and hence do not quantify endogenous, unmodified protein. Similarly, the tagging can alter protein levels - in some instances hindering protein expression completely (11). Even so, epitope tagging methods have been of value to the community, yielding high coverage quantitative data sets for the majority of the yeast proteome (11, 12). MS-based methods do not rely on such nonendogenous labels, and can reach genome-wide levels of coverage. Accurate estimation of absolute concentrations i.e. protein copy number per cell, also usually necessitates the use of (one or more) external or internal standards from which to derive absolute abundance (4). Examples include a comprehensive quantification of the Leptospira interrogans proteome that used a 19 protein subset quantified using selected reaction monitoring (SRM)1 to calibrate their label-free data (8, 13). It is worth noting that epitope tagging methods, although also absolute, rely on a very limited set of standards for the quantitative western blots and necessitate incorporation of a suitable immunogenic tag (11). Other recent, innovative approaches exploiting total ion signal and internal scaling to estimate protein cellular abundance (10, 14), avoid the use of internal standards, though they do rely on targeted proteomic data to validate their approach. The use of targeted SRM strategies to derive proteomic calibration standards highlights its advantages in comparison to label-free in terms of accuracy, precision, dynamic range and limit of detection and has gained currency for its reliability and sensitivity (3, 15⇓–17). Indeed, SRM is often referred to as the “gold standard proteomic quantification method,” being particularly well-suited when the proteins to be quantified are known, when appropriate surrogate peptides for protein quantification can be selected a priori, and matched with stable isotope-labeled (SIL) standards (18⇓–20). In combination with SIL peptide standards that can be generated through a variety of means (3, 15), SRM can be used to quantify low copy number proteins, reaching down to ∼50 cpc in yeast (5). However, although SRM methodology has been used extensively for S. cerevisiae protein quantification by us and others (19, 21, 22), it has not been used for large protein cohorts because of the requirement to generate the large numbers of attendant SIL peptide standards; the largest published data set is only for a few tens of proteins. It remains a challenge therefore to robustly quantify an entire eukaryotic proteome in absolute terms by direct means using targeted MS and this is the focus of our present study, the Census Of the Proteome of Yeast (CoPY). We present here direct and absolute quantification of nearly 2000 endogenous proteins from S. cerevisiae grown in steady state in a chemostat culture, using the SRM-based QconCAT approach. Although arguably not quantification of the entire proteome, this represents an accurate and rigorous collection of direct yeast protein quantifications, providing a gold-standard data set of endogenous protein levels for future reference and comparative studies. The highly reproducible SIL-SRM MS data, with robust CVs typically less than 20%, is compared with other extant data sets that were obtained via alternative analytical strategies. We also report a matched high quality transcriptome from the same cells using RNA-seq, which supports additional calculations including a refined estimate of the total protein content in yeast cells, and a simple linear model of translation explaining 70% of the variance between RNA and protein levels in yeast chemostat cultures. These analyses confirm the validity of our data and approach, which we believe represents a state-of-the-art absolute quantification compendium of a significant proportion of a model eukaryotic proteome