Geometric effects of a quarter of corrugated torus

In the spirit of the thin-layer quantization scheme, we give the effective Shr\"{o}dinger equation for a particle confined to a corrugated torus, in which the geometric potential is substantially changed by corrugation. We find the attractive wells reconstructed by the corrugation not being at identical depths, which is strikingly different from that of a corrugated nanotube, especially in the inner side of the torus. By numerically calculating the transmission probability, we find that the resonant tunneling peaks and the transmission gaps are merged and broadened by the corrugation of the inner side of torus. These results show that the quarter corrugated torus can be used not only to connect two tubes with different radiuses in different directions, but also to filter the particles with particular incident~energies.Comment: 7 pages, 8 figure

Stochastic regret minimization for revenue management problems with nonstationary demands

We study an admission control model in revenue management with nonstationary and correlated demands over a finite discrete time horizon. The arrival probabilities are updated by current available information, that is, past customer arrivals and some other exogenous information. We develop a regret‐based framework, which measures the difference in revenue between a clairvoyant optimal policy that has access to all realizations of randomness a priori and a given feasible policy which does not have access to this future information. This regret minimization framework better spells out the trade‐offs of each accept/reject decision. We proceed using the lens of approximation algorithms to devise a conceptually simple regret‐parity policy. We show the proposed policy achieves 2‐approximation of the optimal policy in terms of total regret for a two‐class problem, and then extend our results to a multiclass problem with a fairness constraint. Our goal in this article is to make progress toward understanding the marriage between stochastic regret minimization and approximation algorithms in the realm of revenue management and dynamic resource allocation. © 2016 Wiley Periodicals, Inc. Naval Research Logistics 63: 433–448, 2016Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/135128/1/nav21704.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/135128/2/nav21704_am.pd

(Z)-1-Phenyl-3-(3-pyridyl­meth­ylamino)­but-2-en-1-one

The reaction of 3-C5H4NCH2NH2 and C6H5COCH2COCH3 affords the title compound, C16H16N2O. The O=C—C=C—N portion is essentially planar [maximum deviation = 0.046 (2) Å] and is aligned at dihedral angles of 22.6 (1) and 78.9 (1)° to the phenyl and pyridyl rings, respectively. The N—H and O=C groups are linked by an intra­molecular hydrogen bond. In the crystal, C—H⋯O hydrogen bonds and C—H⋯π inter­actions occur

The role of thrombomodulin lectin-like domain in inflammation

Thrombomodulin (TM) is a cell surface glycoprotein which is widely expressed in a variety of cell types. It is a cofactor for thrombin binding that mediates protein C activation and inhibits thrombin activity. In addition to its anticoagulant activity, recent evidence has revealed that TM, especially its lectin-like domain, has potent anti-inflammatory function through a variety of molecular mechanisms. The lectin-like domain of TM plays an important role in suppressing inflammation independent of the TM anticoagulant activity. This article makes an extensive review of the role of TM in inflammation. The molecular targets of TM lectin-like domain have also been elucidated. Recombinant TM protein, especially the TM lectin-like domain may play a promising role in the management of sepsis, glomerulonephritis and arthritis. These data demonstrated the potential therapeutic role of TM in the treatment of inflammatory diseases

Correlation Analysis for Protein Evolutionary Family Based on Amino Acid Position Mutations and Application in PDZ Domain

BACKGROUND: It has been widely recognized that the mutations at specific directions are caused by the functional constraints in protein family and the directional mutations at certain positions control the evolutionary direction of the protein family. The mutations at different positions, even distantly separated, are mutually coupled and form an evolutionary network. Finding the controlling mutative positions and the mutative network among residues are firstly important for protein rational design and enzyme engineering. METHODOLOGY: A computational approach, namely amino acid position conservation-mutation correlation analysis (CMCA), is developed to predict mutually mutative positions and find the evolutionary network in protein family. The amino acid position mutative function, which is the foundational equation of CMCA measuring the mutation of a residue at a position, is derived from the MSA (multiple structure alignment) database of protein evolutionary family. Then the position conservation correlation matrix and position mutation correlation matrix is constructed from the amino acid position mutative equation. Unlike traditional SCA (statistical coupling analysis) approach, which is based on the statistical analysis of position conservations, the CMCA focuses on the correlation analysis of position mutations. CONCLUSIONS: As an example the CMCA approach is used to study the PDZ domain of protein family, and the results well illustrate the distantly allosteric mechanism in PDZ protein family, and find the functional mutative network among residues. We expect that the CMCA approach may find applications in protein engineering study, and suggest new strategy to improve bioactivities and physicochemical properties of enzymes