Indirect exchange of magnetic impurities in zigzag graphene ribbon

We use quantum Monte Carlo method to study the indirect coupling between two magnetic impurities on the zigzag edge of graphene ribbon, with respect to the chemical potential $\mu$. We find that the spin-spin correlation between two adatoms located on the nearest sites in the zigzag edge are drastically suppressed around the zero-energy. As we switch the system away from half-filling, the antiferromagnetic correlation is first enhanced and then decreased. If the two adatoms are adsorbed on the sites belonging to the same sublattice, we find similar behavior of spin-spin correlation except for a crossover from ferromagnetic to antiferromagentic correlation in the vicinity of zero-energy. We also calculated the weight of different components of d-electron wave function and local magnet moment for various values of parameters, and all the results are consistent with those of spin-spin correlation between two magnetic impurities.Comment: 3 pages, 4 figures, conference proceedin

H2A.Z facilitates access of active and repressive complexes to chromatin in embryonic stem cell self-renewal and differentiation.

SummaryChromatin modifications have been implicated in the self-renewal and differentiation of embryonic stem cells (ESCs). However, the function of histone variant H2A.Z in ESCs remains unclear. We show that H2A.Z is highly enriched at promoters and enhancers and is required for both efficient self-renewal and differentiation of murine ESCs. H2A.Z deposition leads to an abnormal nucleosome structure, decreased nucleosome occupancy, and increased chromatin accessibility. In self-renewing ESCs, knockdown of H2A.Z compromises OCT4 binding to its target genes and leads to decreased binding of MLL complexes to active genes and of PRC2 complex to repressed genes. During differentiation of ESCs, inhibition of H2A.Z also compromises RA-induced RARα binding, activation of differentiation markers, and the repression of pluripotency genes. We propose that H2A.Z mediates such contrasting activities by acting as a general facilitator that generates access for a variety of complexes, both activating and repressive

Quantifying the Effect of Registration Error on Spatio-Temporal Fusion

It is challenging to acquire satellite sensor data with both fine spatial and fine temporal resolution, especially for monitoring at global scales. Among the widely used global monitoring satellite sensors, Landsat data have a coarse temporal resolution, but fine spatial resolution, while moderate resolution imaging spectroradiometer (MODIS) data have fine temporal resolution, but coarse spatial resolution. One solution to this problem is to blend the two types of data using spatio-temporal fusion, creating images with both fine temporal and fine spatial resolution. However, reliable geometric registration of images acquired by different sensors is a prerequisite of spatio-temporal fusion. Due to the potentially large differences between the spatial resolutions of the images to be fused, the geometric registration process always contains some degree of uncertainty. This article analyzes quantitatively the influence of geometric registration error on spatio-temporal fusion. The relationship between registration error and the accuracy of fusion was investigated under the influence of different temporal distances between images, different spatial patterns within the images and using different methods (i.e., spatial and temporal adaptive reflectance fusion model (STARFM), and Fit-FC; two typical spatio-temporal fusion methods). The results show that registration error has a significant impact on the accuracy of spatio-temporal fusion; as the registration error increased, the accuracy decreased monotonically. The effect of registration error in a heterogeneous region was greater than that in a homogeneous region. Moreover, the accuracy of fusion was not dependent on the temporal distance between images to be fused, but rather on their statistical correlation. Finally, the Fit-FC method was found to be more accurate than the STARFM method, under all registration error scenarios. © 2008-2012 IEEE

Supplying Improved Seed to Farmers in Rural Kenya: The Case of Freshco Kenya Ltd.

Freshco, a small producer and distributor of hybrid maize seed and macadamia seedlings, was one of the first private companies to enter the Kenya seed market after its liberalization. Currently, the company produces and markets six high yielding maize varieties that are suited for diverse agro-ecological conditions. Despite the company’s encouraging growth in the local maize seed market, Freshco’s executives recognize the need to scale up operations to stay competitive. The company’s challenge is to recognize business opportunities and customer needs in an environment susceptible to ecological, political, and socioeconomic change.Kenya, seed industry, smallholder farmers, scenario planning, Crop Production/Industries, Farm Management, Research Methods/ Statistical Methods, Q10, Q12,

Hyperon polarization in e^-p --> e^-HK with polarized electron beams

We apply the picture proposed in a recent Letter for transverse hyperon polarization in unpolarized hadron-hadron collisions to the exclusive process e^-p --> e^-HK such as e^-p-->e^-\Lambda K^+, e^-p --> e^-\Sigma^+ K^0, or e^-p--> e^-\Sigma^0 K^+, or the similar process e^-p\to e^-n\pi^+ with longitudinally polarized electron beams. We present the predictions for the longitudinal polarizations of the hyperons or neutron in these reactions, which can be used as further tests of the picture.Comment: 15 pages, 2 figures. submitted to Phys. Rev.

Cloning and homologic analysis of Tpn I gene in silkworm Bombyx mori

The troponin complex is composed of three subunits, Troponin C (the calcium sensor component) and Troponin T and I (structural proteins). Tpn C is encoded by multiple genes in insects, while the Tpn T and Tpn I proteins are encoded by single genes. Tpn I binds to actin and Tpn T binds to tropomyosin. We cloned and sequenced the Tpn I (AY873787) gene from Bombyx mori that encodes 225 amino acids and contains a conserved motif seen in Drosophila virilis and Anopheles gambiae. Bioinformaticanalysis suggests that its deduced amino sequence shares 81.3 and 78.7% homology with the Tpn I genes of A. gambiae and D. virili, respectively