Optimal classical-communication-assisted local model of n-qubit Greenberger-Horne-Zeilinger correlations

We present a model, motivated by the criterion of reality put forward by Einstein, Podolsky, and Rosen and supplemented by classical communication, which correctly reproduces the quantum-mechanical predictions for measurements of all products of Pauli operators on an n-qubit GHZ state (or ``cat state''). The n-2 bits employed by our model are shown to be optimal for the allowed set of measurements, demonstrating that the required communication overhead scales linearly with n. We formulate a connection between the generation of the local values utilized by our model and the stabilizer formalism, which leads us to conjecture that a generalization of this method will shed light on the content of the Gottesman-Knill theorem.Comment: New version - expanded and revised to address referee comment

Oligosaccharide model of the vascular endothelial glycocalyx in physiological flow

Experiments have consistently revealed the pivotal role of the endothelial glycocalyx layer in vasoregulation and the layer’s contribution to mechanotransduction pathways. However, the exact mechanism by which the glycocalyx mediates fluid shear stress remains elusive. This study employs atomic-scale molecular simulations with the aim of investigating the conformational and orientation properties of highly flexible oligosaccharide components of the glycocalyx and their suitability as transduction molecules under hydrodynamic loading. Fluid flow was shown to have nearly no effect on the conformation populations explored by the oligosaccharide, in comparison with static (diffusion) conditions. However, the glycan exhibited a significant orientation change, when compared to simple diffusion, aligning itself with the flow direction. It is the tethered end of the glycan, an asparagine amino acid, which experienced conformational changes as a result of this flow-induced bias. Our results suggest that shear flow through the layer can have an impact on the conformational properties of saccharide-decorated transmembrane proteins, thus acting as a mechanosensor

Thickness-dependent thermal properties of amorphous insulating thin films measured by photoreflectance microscopy

In this work, we report on the measurement of the thermal conductivity of thin insulating films of SiO2 obtained by thermal oxidation, and Al2O3 grown by atomic layer deposition (ALD), both on Si wafers. We used photoreflectance microscopy to determine the thermal properties of the films as a function of thickness in the 2 nm to 1000 nm range. The effective thermal conductivity of the Al2O3 layer is shown to decrease with thickness down to 70% for the thinnest layers. The data were analyzed upon considering that the change in the effective thermal conductivity corresponds to an intrinsic thermal conductivity associated to an additional interfacial thermal resistance. The intrinsic conductivity and interfacial thermal resistance of SiO2 were found to be equal to 0.95 W/m·K and 5.1 × 10− 9 m2K/W respectively; those of Al2O3 were found to be 1.56 W/m·K and 4.3 × 10− 9 m2K/W

The quadrupole resonator: Construction, RF System Field Calculations and First Applications

The quadrupole resonator allows measurement of the RF properties of superconducting (sc) films deposited on disk-shaped metallic substrates. We describe the construction of the apparatus, the brazing and electron-beam welding procedures, the arrangements for compensating mechanical tolerances of samples and for assuring reproducible sample illumination. We explain the special features of the RF sy stem and give the results of field calculations with a 3D cavity code. Finally we present first measurements of Nb on Cu film samples and compare them with calibrations done with a bulk Nb sample

Directed evolution methods for overcoming trade‐offs between protein activity and stability

Engineered proteins are being widely developed and employed in applications ranging from enzyme catalysts to therapeutic antibodies. Directed evolution, an iterative experimental process composed of mutagenesis and library screening, is a powerful technique for enhancing existing protein activities and generating entirely new ones not observed in nature. However, the process of accumulating mutations for enhanced protein activity requires chemical and structural changes that are often destabilizing, and low protein stability is a significant barrier to achieving large enhancements in activity during multiple rounds of directed evolution. Here we highlight advances in understanding the origins of protein activity/stability trade‐offs for two important classes of proteins (enzymes and antibodies) as well as innovative experimental and computational methods for overcoming such trade‐offs. These advances hold great potential for improving the generation of highly active and stable proteins that are needed to address key challenges related to human health, energy and the environment.Peer Reviewedhttps://deepblue.lib.umich.edu/bitstream/2027.42/154495/1/aic16814_am.pdfhttps://deepblue.lib.umich.edu/bitstream/2027.42/154495/2/aic16814.pd