The gap exponent of XXZ model in a transverse field

We have calculated numerically the gap exponent of the anisotropic Heisenberg model in the presence of the transverse magnetic field. We have implemented the modified Lanczos method to obtain the excited states of our model with the same accuracy of the ground state. The coefficient of the leading term in the perturbation expansion diverges in the thermodynamic limit (N --> infinity). We have obtained the relation between this divergence and the scaling behaviour of the energy gap. We have found that the opening of gap in the presence of transverse field scales with a critical exponent which depends on the anisotropy parameter (Delta). Our numerical results are in well agreement with the field theoretical approach in the whole range of the anisotropy parameter, -1 < Delta < 1.Comment: 6 pages and 4 figure

Phase Transitions in Bilayer Heisenberg Model with General Couplings

The ground state properties and phase diagram of the bilayer square-lattice Heisenberg model are studied in a broad parameter space of intralayer exchange couplings, assuming an antiferromagnetic coupling between constituent layers. In the classical limit, the model exhibits three phases: two of these are ordered phases specified by the ordering wave vectors (pi,pi;pi) and (0,0;pi), where the third component of each indecates the antiferromagnetic orientation between layers, while another one is a canted phase, stabilized by competing interactions. The effects of quantum fluctuations in the model with S=1/2 have been explored by means of dimer mean-field theory, small-system exact diagonalization, and high-order perturbation expansions about the interlayer dimer limit.Comment: 15 pages, LaTeX, 12 figures, uses jpsj.sty, revised version: some discussion to a related model and references added, submitted to the Journal of the Physical Society of Japa

Ambient Stable Quantitative PCR Reagents for the Detection of Yersinia pestis

Plague, caused by Yersinia pestis, is one of the oldest and most dangerous diseases in human history, and has claimed millions of lives in the three major historical pandemics. Although panic caused by the Black Death is fading, the threat of the reemergence of plague pandemics still exists, with the additional potential of misuse in biowarfare or bioterrorism. Rapid on-site detection and identification of the pathogen is of paramount significance for timely implementation of effective countermeasures. TaqMan probe-based real-time PCR assays can give quick and accurate identification; however, the need for cold delivery and storage prevents its potential on-site application. The objective of this study was to develop a stable PCR system for easy delivery and storage under room temperature, which is vital for conventional plague surveillance and for preparedness in public health emergencies. We present a solution to this particular issue, hoping that it is helpful to future applications

A short sequence for the iterative synthesis of fused polyethers

A simple and efficient four‐step sequence for the synthesis of fused polyether arrays has been developed. Cyclic ethers are installed by sequential alkynyl ether formation, carbocupration, ring‐closing metathesis and hydroboration with acidic workup. Crucially, the alkene required for the subsequent ring formation by ring‐closing metathesis is present in the substrate but is masked in the form of a vinylic silane, which prevents competitive metathesis of the side chain. Generation of the reactive alkene from the unreactive vinylic silane is accomplished by hydroboration and subsequent acid‐mediated Peterson elimination of the intermediate hydroxysilane

Free Cysteine Modulates the Conformation of Human C/EBP Homologous Protein

The C/EBP Homologous Protein (CHOP) is a nuclear protein that is integral to the unfolded protein response culminating from endoplasmic reticulum stress. Previously, CHOP was shown to comprise extensive disordered regions and to self-associate in solution. In the current study, the intrinsically disordered nature of this protein was characterized further by comprehensive in silico analyses. Using circular dichroism, differential scanning calorimetry and nuclear magnetic resonance, we investigated the global conformation and secondary structure of CHOP and demonstrated, for the first time, that conformational changes in this protein can be induced by the free amino acid l-cysteine. Addition of l-cysteine caused a significant dose-dependent decrease in the protein helicity – dropping from 69.1% to 23.8% in the presence of 1 mM of l-cysteine – and a sequential transition to a more disordered state, unlike that caused by thermal denaturation. Furthermore, the presence of small amounts of free amino acid (80 µM, an 8∶1 cysteine∶CHOP ratio) during CHOP thermal denaturation altered the molecular mechanism of its melting process, leading to a complex, multi-step transition. On the other hand, high levels (4 mM) of free l-cysteine seemed to cause a complete loss of rigid cooperatively melting structure. These results suggested a potential regulatory function of l-cysteine which may lead to changes in global conformation of CHOP in response to the cellular redox state and/or endoplasmic reticulum stress