Effect of epitaxial strain on ferroelectric polarization in multiferroic BiFeO3 films

Multiferroic BiFeO3 epitaxial films with thickness ranging from 40 nm to 960 nm were grown by pulsed laser deposition on SrTiO3 (001) substrates with SrRuO3 bottom electrodes. X-ray characterization shows that the structure evolves from angularly-distorted tetragonal with c/a ~ 1.04 to more bulk-like distorted rhombohedral (c/a ~ 1.01) as the strain relaxes with increasing thickness. Despite this significant structural evolution, the ferroelectric polarization along the body diagonal of the distorted pseudo-cubic unit cells, as calculated from measurements along the normal direction, barely changes.Comment: Legend in Fig.3 corrected and et

Generic Lightlike Submanifolds of an Indefinite Cosymplectic Manifold

Lightlike geometry has its applications in general relativity, particularly in black hole theory. Indeed, it is known that lightlike hypersurfaces are examples of physical models of Killing horizons in general relativity (Galloway, 2007). In this paper, we introduce the definition of generic lightlike submanifolds of an indefinite cosymplectic manifold. We investigate new results on a class of generic lightlike submanifolds of an indefinite cosymplectic manifold

A Basic Inequality for the Tanaka-Webster Connection

For submanifolds tangent to the structure vector field in Sasakian space forms, we establish a Chen's basic inequality between the main intrinsic invariants of the submanifold (namely, its pseudosectional curvature and pseudosectional curvature on one side) and the main extrinsic invariant (namely, squared pseudomean curvature on the other side) with respect to the Tanaka-Webster connection. Moreover, involving the pseudo-Ricci curvature and the squared pseudo-mean curvature, we obtain a basic inequality for submanifolds of a Sasakian space form tangent to the structure vector field in terms of the Tanaka-Webster connection

Folding machineries displayed on a cation-exchanger for the concerted refolding of cysteine- or proline-rich proteins

<p>Abstract</p> <p>Background</p> <p><it>Escherichia coli </it>has been most widely used for the production of valuable recombinant proteins. However, over-production of heterologous proteins in <it>E. coli </it>frequently leads to their misfolding and aggregation yielding inclusion bodies. Previous attempts to refold the inclusion bodies into bioactive forms usually result in poor recovery and account for the major cost in industrial production of desired proteins from recombinant <it>E. coli</it>. Here, we describe the successful use of the immobilized folding machineries for <it>in vitro </it>refolding with the examples of high yield refolding of a ribonuclease A (RNase A) and cyclohexanone monooxygenase (CHMO).</p> <p>Results</p> <p>We have generated refolding-facilitating media immobilized with three folding machineries, mini-chaperone (a monomeric apical domain consisting of residues 191–345 of GroEL) and two foldases (DsbA and human peptidyl-prolyl <it>cis-trans </it>isomerase) by mimicking oxidative refolding chromatography. For efficient and simple purification and immobilization simultaneously, folding machineries were fused with the positively-charged consecutive 10-arginine tag at their C-terminal. The immobilized folding machineries were fully functional when assayed in a batch mode. When the refolding-facilitating matrices were applied to the refolding of denatured and reduced RNase A and CHMO, both of which contain many cysteine and proline residues, RNase A and CHMO were recovered in 73% and 53% yield of soluble protein with full enzyme activity, respectively.</p> <p>Conclusion</p> <p>The refolding-facilitating media presented here could be a cost-efficient platform and should be applicable to refold a wide range of <it>E. coli </it>inclusion bodies in high yield with biological function.</p

Solutions of xqk+⋯+xq+x=ax^{q^k}+\cdots+x^{q}+x=a in GF2nGF{2^n}

Though it is well known that the roots of any affine polynomial over a finite field can be computed by a system of linear equations by using a normal base of the field, such solving approach appears to be difficult to apply when the field is fairly large. Thus, it may be of great interest to find an explicit representation of the solutions independently of the field base. This was previously done only for quadratic equations over a binary finite field. This paper gives an explicit representation of solutions for a much wider class of affine polynomials over a binary prime field

Determinants of Visitor’s Overnight Stay in Local Food Festival: An Exploration of Staycation Concept and It’s Relation to the Origin of Visitors

The primary aim of this study was to explore the determinants of tourist overnight stay at a destination. The data was collected through a questionnaire conducted in two local food festivals in the Mid-west area in the U.S in 2010. The results of this study has both industry and academia implications; this study reveals the geographical distance (i.e., minimum of 100 miles away) that is most beneficial in obtaining overnight stays

Molecular cloning and biochemical characterization of a novel erythrose reductase from Candida magnoliae JH110

<p>Abstract</p> <p>Background</p> <p>Erythrose reductase (ER) catalyzes the final step of erythritol production, which is reducing erythrose to erythritol using NAD(P)H as a cofactor. ER has gained interest because of its importance in the production of erythritol, which has extremely low digestibility and approved safety for diabetics. Although ERs were purified and characterized from microbial sources, the entire primary structure and the corresponding DNA for ER still remain unknown in most of erythritol-producing yeasts. <it>Candida magnoliae </it>JH110 isolated from honeycombs produces a significant amount of erythritol, suggesting the presence of erythrose metabolizing enzymes. Here we provide the genetic sequence and functional characteristics of a novel NADPH-dependent ER from <it>C. magnoliae </it>JH110.</p> <p>Results</p> <p>The gene encoding a novel ER was isolated from an osmophilic yeast <it>C. magnoliae </it>JH110. The ER gene composed of 849 nucleotides encodes a polypeptide with a calculated molecular mass of 31.4 kDa. The deduced amino acid sequence of ER showed a high degree of similarity to other members of the aldo-keto reductase superfamily including three ER isozymes from <it>Trichosporonoides megachiliensis </it>SNG-42. The intact coding region of ER from <it>C. magnoliae </it>JH110 was cloned, functionally expressed in <it>Escherichia coli </it>using a combined approach of gene fusion and molecular chaperone co-expression, and subsequently purified to homogeneity. The enzyme displayed a temperature and pH optimum at 42°C and 5.5, respectively. Among various aldoses, the <it>C. magnoliae </it>JH110 ER showed high specific activity for reduction of erythrose to the corresponding alcohol, erythritol. To explore the molecular basis of the catalysis of erythrose reduction with NADPH, homology structural modeling was performed. The result suggested that NADPH binding partners are completely conserved in the <it>C. magnoliae </it>JH110 ER. Furthermore, NADPH interacts with the side chains Lys252, Thr255, and Arg258, which could account for the enzyme's absolute requirement of NADPH over NADH.</p> <p>Conclusions</p> <p>A novel ER enzyme and its corresponding gene were isolated from <it>C. magnoliae </it>JH110. The <it>C. magnoliae </it>JH110 ER with high activity and catalytic efficiency would be very useful for <it>in vitro </it>erythritol production and could be applied for the production of erythritol in other microorganisms, which do not produce erythritol.</p