Periodic pattern formation in reaction-diffusion systems -an introduction for numerical simulation

The aim of the present review is to provide a comprehensive explanation of Turing reaction–diffusion systems in sufficient detail to allow readers to perform numerical calculations themselves. The reaction–diffusion model is widely studied in the field of mathematical biology, serves as a powerful paradigm model for self-organization and is beginning to be applied to actual experimental systems in developmental biology. Despite the increase in current interest, the model is not well understood among experimental biologists, partly because appropriate introductory texts are lacking. In the present review, we provide a detailed description of the definition of the Turing reaction–diffusion model that is comprehensible without a special mathematical background, then illustrate a method for reproducing numerical calculations with Microsoft Excel. We then show some examples of the patterns generated by the model. Finally, we discuss future prospects for the interdisciplinary field of research involving mathematical approaches in developmental biology

ECONOMIC RISK AND THE STRUCTURAL CHARACTERISTICS OF FARM BUSINESSES

Using longitudinal panel farm-level data, this study finds that income variability may be materially influenced by farm size. Econometric results suggest that policy analyses and other considerations of the distributional effects of, and response to, income variability for commercial scale family farms may concentrate on farm size and other structural variables.risk, income variability, farm size, financial structure, Farm Management, Industrial Organization,

Nonpolar resistive switching in Cu/SiC/Au non-volatile resistive memory devices

Amorphous silicon carbide (a-SiC) based resistive memory (RM) Cu/a-SiC/Au devices were fabricated and their resistive switching characteristics investigated. All four possible modes of nonpolar resistive switching were achieved with ON/OFF ratio in the range 10 6-10 8. Detailed current-voltage I-V characteristics analysis suggests that the conduction mechanism in low resistance state is due to the formation of metallic filaments. Schottky emission is proven to be the dominant conduction mechanism in high resistance state which results from the Schottky contacts between the metal electrodes and SiC. ON/OFF ratios exceeding 10 7 over 10 years were also predicted from state retention characterizations. These results suggest promising application potentials for Cu/a-SiC/Au RM

An epidemic of enteric fever spread by personal infection in an asylum

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The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process.

Formation of misfolded aggregates is an essential part of what proteins can do. The process of protein aggregation is central to many human diseases and any aggregating event needs to be prevented within a cell and in protein design. In order to aggregate, a protein needs to unfold its native state, at least partially. The conformational state that is prone to aggregate is difficult to study, due to its aggregating potential and heterogeneous nature. Here, we use a systematic approach of limited proteolysis, in combination with electrospray ionisation mass spectrometry, to investigate the regions that are most flexible and solvent-exposed within the native, ligand-bound and amyloidogenic states of muscle acylphosphatase (AcP), a protein previously shown to form amyloid fibrils in the presence of trifluoroethanol. Seven proteases with different degrees of specificity have been used for this purpose. Following exposure to the aggregating conditions, a number of sites along the sequence of AcP become susceptible to proteolytic digestion. The pattern of proteolytic cleavages obtained under these conditions is considerably different from that of the native and ligand-bound conformations and includes a portion within the N-terminal tail of the protein (residues 6-7), the region of the sequence 18-23 and the position 94 near the C terminus. There is a significant overlap between the regions of the sequence found to be solvent-exposed from the present study and those previously identified to be critical in the rate-determining steps of aggregation from protein engineering approaches. This indicates that a considerable degree of solvent exposure is a feature of the portions of a protein that initiate the process of aggregation