Observation of B̅0→D(*)0pp̅

journal articl

三相3線-三相4線式昇圧形マトリクスコンバータの出力電圧一定制御

application/pdf三重大学大学院 工学研究科 博士前期課程 電気電子工学専攻 電気システム工学講座75pthesi

Mechanism of Corrugated Graphene Moiré Superstructures on Transition-Metal Surfaces

A graphene layer on a transition-metal (TM) surface can be either corrugated or flat, depending on the type of the substrate and its rotation angle with respect to the substrate. It was broadly observed that the degree of corrugation generally decreases with the increase of rotation angle or the decrease of Moiré pattern size. In contrast to a flat graphene on a TM surface, a corrugated graphene layer has an increased binding energy to the substrate and a concomitant elastic energy. Here, we developed a theoretical model about the competition between the binding energy increase and the elastic energy of corrugated graphene layers on TM surfaces in which all the parameters can be calculated by density functional theory (DFT) calculations. The agreement between the theoretical model and the experimental observations of graphene on various TM surfaces, for example, Ru(0001), Rh(111), Pt(111), and Ir(111), substantiated the applicability of this model for graphene on other TM surfaces. Moreover, the morphology of a graphene layer on an arbitrary TM surface can be theoretically predicted through simple DFT calculations based on the model. Our work thus provides a theoretical framework for the intelligent design of graphene/TM superstructures with the desired structure

Substrate Screening for the Epitaxial Growth of a Single-Crystal Graphene Wafer

Epitaxial growth of a two-dimensional (2D) single crystal necessitates the symmetry group of the substrate being a subgroup of that of the 2D material. As a consequence of the theory of 2D material epitaxy, high-index surfaces, which own very low symmetry, have been successfully used to grow various 2D single crystals, while the rule of selecting the best substrates for 2D single crystal growth is still absent. Here, extensive density functional theory calculations were conducted to investigate the growth of graphene on abundant high-index Cu substrates. Although step edges are commonly regarded as the most active sites for graphene nucleation, our study reveals that, in some cases, graphene nucleation on terraces is superior than that near a step edge. To achieve parallel alignments of graphene islands, it is essential to either suppress terrace nucleation or ensure consistent orientations templated by both the terrace and step edge. In agreement with most experimental observations, we show that Cu substrates for the growth of single-crystalline graphene include vicinal Cu(111) surfaces, vicinal Cu(110) surfaces with Miller indices of (nn1) (n > 3), and vicinal Cu(100) surfaces with Miller indices of (n11) (n > 3)

Additional file 2 of Integrated identification of key genes and pathways in Alzheimer’s disease via comprehensive bioinformatical analyses

Table S2. Information for the DEGs identified from the GEO dataset (|log2FC| ≥ 1, p value< 0.05). Included detailed information of all DEGs screened from hippocampus and entorhinal cortex regions. (XLSX 31 kb

Additional file 3 of Integrated identification of key genes and pathways in Alzheimer’s disease via comprehensive bioinformatical analyses

Table S3. Information for biological process analysis of DEGs from hippocampus. Included detailed information of results of biological process analysis of DEGs from hippocampus. (XLSX 32 kb

Hydrophobic/Hydrophilic Ratio of Amphiphilic Helix Mimetics Determines the Effects on Islet Amyloid Polypeptide Aggregation

Amyloid depositions of human islet amyloid polypeptides (hIAPP) are associated with type II diabetes (T2D) impacting millions of people globally. Accordingly, strategies against hIAPP aggregation are essential for the prevention and eventual treatment of the disease. Helix mimetics, which modulate the protein–protein interaction by mimicking the side chain residues of a natural α-helix, were found to be a promising strategy for inhibiting hIAPP aggregation. Here, we applied molecular dynamics simulations to investigate two helix mimetics reported to have opposite effects on hIAPP aggregation in solution, the oligopyridylamide-based scaffold 1e promoted, whereas naphthalimide-appended oligopyridylamide scaffold DM 1 inhibited the aggregation of hIAPP in solution. We found that 1e promoted hIAPP aggregation because of the recruiting effects through binding with the N-termini of hIAPP peptides. In contrast, DM 1 with a higher hydrophobic/hydrophilic ratio effectively inhibited hIAPP aggregation by strongly binding with the C-termini of hIAPP peptides, which competed for the interpeptide contacts between amyloidogenic regions in the C-termini and impaired the fibrillization of hIAPP. Structural analyses revealed that DM 1 formed the core of hIAPP-DM 1 complexes and stabilized the off-pathway oligomers, whereas 1e formed the corona outside the hIAPP-1e complexes and remained active in recruiting free hIAPP peptides. The distinct interaction mechanisms of DM 1 and 1e, together with other reported potent antagonists in the literature, emphasized the effective small molecule-based amyloid inhibitors by disrupting peptide interactions that should reach a balanced hydrophobic/hydrophilic ratio, providing a viable and generic strategy for the rational design of novel anti-amyloid nanomedicine

Additional file 6 of Integrated identification of key genes and pathways in Alzheimer’s disease via comprehensive bioinformatical analyses

Table S6. Information for biological process analysis of DEGs from entorhinal cortex. Included detailed information of results of biological process analysis of DEGs from entorhinal cortex. (XLSX 16 kb

Additional file 4 of Integrated identification of key genes and pathways in Alzheimer’s disease via comprehensive bioinformatical analyses

Table S4. Information for cellular component analysis of DEGs from hippocampus. Included detailed information of results of cellular component analysis of DEGs from hippocampus. (XLSX 21 kb

The Sequence Entropy Computed from Simulations versus the Naturally Occurring Sequence Entropy Computed from HSSP

<p>Three families of protein homologs were studied: HPR domain (A,D,G), ROSSMAN fold (B,E,H), and SH3 domain (C,F,I). The open circles (○) in (A–F) correspond to the functionally important residues. In (G–I), these functionally important residues are shown in stick representation. In (G,H), the SO₄²⁻ ions are used to mimic the phosphate anion in crystal preparation. In (I), the poly-proline peptide are shown in yellow and the peptide-binding residues form a continuous surface, shown in mesh representation.</p