Shibusawa Eiichi\u27s View of Japan\u27s Foreign Affairs: Focusing on His Influences on the Meiji Government

From the mid-nineteenth century, Asia, including China and Japan, has been involved in the trend of modernization that was triggered by the activities of European and American powers in this area. In a time of drastic changes, Shibusawa Eiichi (1840-1931) assumed several roles successively: he served as retainer during the bakumatsu period, as official in the Meiji government, and afterwards as businessman, philanthropist, and non-official diplomat. During his service in the Meiji government from 1869 to 1873 and as an entrepreneur from 1873 to 1909, Shibusawa played a key role in devising economic and diplomatic policies for the Meiji government. He is even considered a major designer of modem Japanese economic systems and society. This paper examines Shibusawa Eiichi\u27s view of Japan\u27s foreign affairs and focuses on the way he influenced the Meiji government

Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus

© 2018, Springer Nature B.V. Ribosome binding factor A (RbfA) is a 14.9 kDa adaptive protein of cold shock, which is important for bacterial growth at low temperatures. RbfA can bind to the free 30S ribosomal subunit and interacts with the 5′-terminal helix (helix I) of 16S rRNA. RbfA is important for the efficient processing of 16S rRNA and for the maturation (assembly) of 30S ribosomal subunits. Here we report backbone and side chains 1H, 13C and 15N chemical shift assignments of RbfA from Staphylococcus aureus. Analysis of the backbone chemical shifts by TALOS+ suggests that RbfA contains four α-helixes and three β-strands with α1-β1-β2-α2-α3-β3-α4 topology. Secondary structure of RbfA have KH-domain fold topology with βααβ subunit which is characterized by a helix-kink-helix motif in which the GxxG sequence is replaced by a conserved AxG sequence, where an Ala residue at position 70 forming an interhelical kink. The solution of the structure of this protein factor and its complex with the ribosome by NMR spectroscopy, X-ray diffraction analysis and cryo-electron microscopy will allow further development of highly selective substances for slowing or completely stopping the translation of the pathogenic bacterium S. aureus, which will interfere with the synthesis and isolation of its pathogenicity factors

Structure of amyloid-beta peptides in a complex-with model membranes

Structures of amyloid-beta peptides Aβ1-40. Aβ10-35, β13-23 and Aβ16-22 in a complex with model membranes in solution were obtained on the analysis of NMR experimental data. It has been established that the process of peptide-micelle complex formation occurs through the amino acid residues LI7, F19, F20 and G29-M35

Structure of amyloid-beta peptides in a complex with model membranes

Structures of amyloid-beta peptides Aβ1-40, Aβ10-35, Aβ13-23 and Aβ16-22 in a complex with model membranes in solution were obtained on the analysis of NMR experimental data. It has been established that the process of peptide-micelle complex formation occurs through the amino acid residues L17, F19, F20 and G29-M35

The effect of the detergent micelles type on the tetrapeptide NAc-SFVG-OMe conformational structure: NMR studies in solution

Process determination of short peptides binding on the cell surface has major implications in better understanding the molecular recognition of cell surfaces. As such methods as on-cell nuclear magnetic resonance (NMR) spectroscopy are very difficult, a large number of membrane mimetic systems such as bilayers, bicelles and detergent micelles use. Micelles are the most frequently used membrane mimetics for the structure determination of peptides and proteins by solution NMR Anionic detergents such as SDS can be more denaturating than the other types, non-ionic micelles being the mildest. Zwitterionic detergent micelles such as DPC are used to mimic eukaryote membranes while the negatively charged SDS micelles would resemble bacterial membranes. Unfortunately, no rules apply when searching for the right detergent. In present paper we studied the effect of the detergent micelles (sodium dodecyl sulfate (SDS) and dodecylphosphocholine (DPC)) on the tetrapeptide SFVG conformational structure. Was shown that the peptide backbone structure is the same in both types of micelles but the sidechain orientation of nonpolar aromatic (Phenylalanine), aliphatic (Glycine) and polar uncharged (Serine) groups are different

Use of a combination of the RDC method and NOESY NMR spectroscopy to determine the structure of Alzheimer's amyloid Aβ10-35 peptide in solution and in SDS micelles

The spatial structure of Alzheimer's amyloid Aβ10-35- NH2 peptide in aqueous solution at pH 7.3 and in SDS micelles was investigated by use of a combination of the residual dipolar coupling method and two-dimensional NMR spectroscopy (TOCSY, NOESY). At pH 7.3 Aβ 10-35-NH2 adopts a compact random-coil conformation whereas in SDS micellar solutions two helical regions (residues 13-23 and 30-35) of Ab10-35-NH2 were observed. By use of experimental data, the structure of "peptide-micelle" complex was determined; it was found that Aβ10-35-NH2 peptide binds to the micelle surface at two regions (residues 17-20 and 29-35).© European Biophysical Societies' Association 2013

NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF)

© 2017 Springer Science+Business Media B.V. Staphylococcus aureus: hibernation-promoting factor (SaHPF) is a 22.2 kDa stationary-phase protein that binds to the ribosome and turns it to the inactive form favoring survival under stress. Sequence analysis has shown that this protein is combination of two homolog proteins obtained in Escherichia coli—ribosome hibernation promoting factor (HPF) (11,000 Da) and ribosome modulation factor RMF (6500 Da). Binding site of E. coli HPF on the ribosome have been shown by X-ray study of Thermus thermophilus ribosome complex. Hence, recent studies reported that the interface is markedly different between 100S from S. aureus and E. coli. Cryo-electron microscopy structure of 100S S. aureus ribosomes reveal that the SaHPF-NTD binds to the 30S subunit as observed for shorter variants of HPF in other species and the C-terminal domain (CTD) protrudes out of each ribosome in order to mediate dimerization. SaHPF-NTD binds to the small subunit similarly to its homologs EcHPF, EcYfiA, and a plastid-specific YfiA. Furthermore, upon binding to the small subunit, the SaHPF-NTD occludes several antibiotic binding sites at the A site (hygromycin B, tetracycline), P site (edeine) and E site (pactamycin, kasugamycin). In order to elucidate the structure, dynamics and function of SaHPF-NTD from S. aureus, here we report the backbone and side chain resonance assignments for SaHPF-NTD. Analysis of the backbone chemical shifts by TALOS+ suggests that SaHPF-NTD contains two α-helices and four β-strands (β1-α1-β2-β3-β4-α2 topology). Investigating the long-term survival of S. aureus and other bacteria under antibiotic pressure could lead to advances in antibiotherapy

NMR structure of the Arctic mutation of the Alzheimer's Aβ(1-40) peptide docked to SDS micelles

© 2014 Elsevier B.V. All rights reserved. The "Arctic" point mutation of the Alzheimer's amyloid β-peptide is a rare mutation leading to an early onset of Alzheimer's disease. The peptide may interact with neuronal membranes, where it can provide its toxic effects. We used 2D NMR spectroscopy to investigate the conformation of the "Arctic" mutant of Aβ1-40 Alzheimer's amyloid peptide in sodium dodecyl sulfate micelle solutions, which are the type of amphiphilic structures mimicking some properties of biomembranes. The study showed that the Arctic mutant of Aβ1-40 interacts with the surface of SDS micelles mainly through the Leu17-Asn27 310-helical region, while the Ile31-Val40 region is buried in the hydrophobic interior of the micelle. In contrast, wild-type Aβ1-40 interacts with SDS micelles through the Lys16-Asp23 α-helical region and Gly29-Met35. Both the Arctic mutant and the wild-type Aβ1-40 peptides interactions with SDS micelles are hydrophobic in nature. Aβ peptides are thought to be capable of forming pores in biomembranes that can cause changes in neuronal and endothelial cell membrane permeability. It has also been shown that Aβ peptides containing the "Arctic" mutation are more neurotoxic and aggregate more readily than the wild-type Aβ peptides at physiological conditions. Here, we propose that the extension of the helical structure of Leu17-Asn27 and a high aliphaticity (neutrality) of the C-terminal region in the Arctic Aβ peptides are consistent with the idea that formation of ion-permeable pores by Aβ oligomers may be one of prevailing mechanisms of a larger neuronal toxicity of the Arctic Aβ compared to the wild-type Aβ peptides, independent of oxidative damage and lipid peroxidation

Mechanism of Neuroprotective Mitochondrial Remodeling by PKA/AKAP1

The mitochondrial signaling complex PKA/AKAP1 protects neurons against mitochondrial fragmentation and cell death by phosphorylating and inactivating the mitochondrial fission enzyme Drp1

NMR Studies of the Mn²⁺ Interactions with Amyloid Peptide Aβ13-23 in Water Environment

© 2016, Springer Science+Business Media New York.In this paper, binding of Mn2+ ions to the fragment of beta-amyloid peptide (Aβ13-23) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide–metal ion binding was made by MnCl2 salt titration and recording 2D 1H–1H NMR TOCSY spectra (TOtal Correlation SpectroscopY). Multidimensional NMR techniques were performed to understand the details of the conformational behavior of the peptide and to reveal the metal-binding sites. According to changes in NMR spectra, the manganese-binding center of the Aβ13-23 peptide is associated with the aspartate residue