Quantum communication cost of preparing multipartite entanglement

We study the preparation and distribution of high-fidelity multi-party entangled states via noisy channels and operations. In the particular case of GHZ and cluster states, we study different strategies using bipartite or multipartite purification protocols. The most efficient strategy depends on the target fidelity one wishes to achieve and on the quality of transmission channel and local operations. We show the existence of a crossing point beyond which the strategy making use of the purification of the state as a whole is more efficient than a strategy in which pairs are purified before they are connected to the final state. We also study the efficiency of intermediate strategies, including sequences of purification and connection. We show that a multipartite strategy is to be used if one wishes to achieve high fidelity, whereas a bipartite strategy gives a better yield for low target fidelity.Comment: 21 pages, 17 figures; accepted for publication in Phys. Rev. A; v2: corrections in figure

A novel and fast purification method for nucleoside transporters

Nucleoside transporters (NTs) play critical biological roles in humans, and to understand the molecular mechanism of nucleoside transport requires high-resolution structural information. However, the main bottleneck for structural analysis of NTs is the production of pure, stable, and high quality native protein for crystallization trials. Here we report a novel membrane protein expression and purification strategy, including construction of a high-yield membrane protein expression vector, and a new and fast purification protocol for NTs. The advantages of this strategy are the improved time efficiency, leading to high quality, active, stable membrane proteins, and the efficient use of reagents and consumables. Our strategy might serve as a useful point of reference for investigating NTs and other membrane proteins by clarifying the technical points of vector construction and improvements of membrane protein expression and purification. © 2016 Hao, Thomsen, Postis, Lesiuk, Sharples, Wang, Bartlam and Goldman.Peer reviewe

On the existence of pure strategy equilibria in large generalized games with atomic players

We consider a game with a continuum of players where only a finite number of them are atomic. Objective functions and admissible strategies may depend on the actions chosen by atomic players and on aggregate information about the actions chosen by non-atomic players. Only atomic players are required to have convex sets of admissible strategies and quasi-concave objective functions. We prove the existence of a pure strategy Nash equilibria. Thus, we extend to large generalized games with atomic players the results of equilibrium existence for non-atomic games of Schemeidler (1973) and Rath (1992). We do not obtain a pure strategy equilibrium by purification of mixed strategy equilibria. Thus, we have a direct proof of both Balder (1999, Theorem 2.1) and Balder (2002, Theorem 2.2.1), for the case where non-atomic players have a common non-empty set of strategies and integrable bounded codification of action profiles. Our main result is readily applicable to many interesting problems in general equilibrium. As an application, we extend Aumann (1966) result on the existence of equilibrium with a continuum of traders to a standard general equilibrium model with incomplete asset markets.Generalized games; Non-convexities; Pure-strategy Nash equilibrium

Automated production of recombinant human proteins as resource for proteome research

<p>Abstract</p> <p>Background</p> <p>An arbitrary set of 96 human proteins was selected and tested to set-up a fully automated protein production strategy, covering all steps from DNA preparation to protein purification and analysis. The target proteins are encoded by functionally uncharacterized open reading frames (ORF) identified by the German cDNA consortium. Fusion proteins were produced in <it>E. coli </it>with four different fusion tags and tested in five different purification strategies depending on the respective fusion tag. The automated strategy relies on standard liquid handling and clone picking equipment.</p> <p>Results</p> <p>A robust automated strategy for the production of recombinant human proteins in <it>E. coli </it>was established based on a set of four different protein expression vectors resulting in NusA/His, MBP/His, GST and His-tagged proteins. The yield of soluble fusion protein was correlated with the induction temperature and the respective fusion tag. NusA/His and MBP/His fusion proteins are best expressed at low temperature (25°C), whereas the yield of soluble GST fusion proteins was higher when protein expression was induced at elevated temperature. In contrast, the induction of soluble His-tagged fusion proteins was independent of the temperature. Amylose was not found useful for affinity-purification of MBP/His fusion proteins in a high-throughput setting, and metal chelating chromatography is recommended instead.</p> <p>Conclusion</p> <p>Soluble fusion proteins can be produced in <it>E. coli </it>in sufficient qualities and μg/ml culture quantities for downstream applications like microarray-based assays, and studies on protein-protein interactions employing a fully automated protein expression and purification strategy. Future applications might include the optimization of experimental conditions for the large-scale production of soluble recombinant proteins from libraries of open reading frames.</p