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

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

Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy

© 2016 European Biophysical Societies' AssociationProtegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong dαα NOE effects between residues R18 and F12, V14, and V16. These “inconsistent” with monomer structure NOEs appears due to formation of an additional antiparallel β-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric β-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data

Spatial structure of heptapeptide Aβ16-22 (beta-amyloid Aβ1-40 active fragment) in solution and in complex with a biological membrane model

The spatial structure of an active fragment of beta-amyloid Aβ1-40 heptapeptide Aβ16-22 (Lys-Leu-Val-Phe- Phe-Ala-Glu) in aqueous buffer solution and in complex with sodium dodecyl sulfate micelles as a model membrane system was investigated by 1H NMR spectroscopy and two-dimensional NMR (TOCSY, HSQC-HECADE (Heteronuclear Couplings from ASSCI-domain experiments with E.COSY-type crosspeaks), NOESY) spectroscopy. Complex formation was confirmed by the chemical shift changes of the heptapeptide's 1H NMR spectra, as well as by the signs and values of the NOE effects in different environments. We compared the spatial structure of the heptapeptide in borate buffer solution and in complex with a model of the cell surface membrane. Copyright © 2012 John Wiley & Sons, Ltd

Spatial Structure of the Decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in Water and in a Complex with Sodium Dodecyl Sulfate Micelles

We have studied the spatial structure of the decapeptide Val-Ile-Lys-Lys-Ser-Thr-Ala-Leu-Leu-Gly in aqueous solution and in a complex with sodium dodecyl sulfate (SDS) micelles by 1H nuclear magnetic resonance (NMR) spectroscopy and two-dimensional (2-D) NMR spectroscopy (total correlation spectroscopy and nuclear Overhauser effect spectroscopy (NOESY)). The approach used to determine the decapeptide spatial structure was based on analysis of the 1H-13C residual dipolar couplings in the molecules partially aligned in lyotropic liquid crystalline media. Analysis of the interproton distances obtained from the 2-D NOESY NMR spectrum was used to reveal the spatial structure of the decapeptide in a complex with SDS micelles. Complex formation was confirmed by analysis of 1H chemical shifts in the NMR spectrum of the decapeptide and analysis of the signs and values of NOEs in a solution with SDS micelles. © 2011 Springer-Verlag

Spatial structure of heptapeptide Glu-Ile-Leu-Asn-His-Met-Lys, a fragment of the HIV enhancer prostatic acid phosphatase, in aqueous and SDS micelle solutions

Prostatic acid phosphatase (PAP) is a protein abundantly present in human seminal fluid. PAP plays important role in fertilization. Its 39-amino-acid fragment, PAP(248-286), is effective in enhancing infectivity of HIV virus. In this work, we determined the spatial structure in aqueous solution of a heptapeptide within the PAP fragment, containing amino acid residues 266-272 (Glu-Ile-Leu-Asn-His-Met-Lys). We also report the structure of the complex formed by this heptapeptide with sodium dodecyl sulfate micelles, a model of a biological membrane, as determined by1H NMR spectroscopy and 2D NMR (TOCSY, HSQC-HECADE, NOESY) spectroscopy. Complex formation was confirmed by chemical shift alterations in the1H NMR spectra of the heptapeptide, as well as by the signs and values of NOE effects. We also present a comparison of the spatial structure of Glu-Ile-Leu-Asn-His-Met-Lys in water and in complex with sodium dodecyl sulfate. © 2012 Elsevier B.V. All rights reserved

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

Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy

© 2016 European Biophysical Societies' AssociationProtegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong dαα NOE effects between residues R18 and F12, V14, and V16. These “inconsistent” with monomer structure NOEs appears due to formation of an additional antiparallel β-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric β-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data

Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy

© 2016 European Biophysical Societies' AssociationProtegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong dαα NOE effects between residues R18 and F12, V14, and V16. These “inconsistent” with monomer structure NOEs appears due to formation of an additional antiparallel β-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric β-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data

Oligomerization of the antimicrobial peptide Protegrin-5 in a membrane-mimicking environment. Structural studies by high-resolution NMR spectroscopy

© 2016, European Biophysical Societies' Association.Protegrin pore formation is believed to occur in a stepwise fashion that begins with a nonspecific peptide interaction with the negatively charged bacterial cell walls via hydrophobic and positively charged amphipathic surfaces. There are five known nature protegrins (PG1-PG5), and early studies of PG-1 (PDB ID:1PG1) shown that it could form antiparallel dimer in membrane mimicking environment which could be a first step for further oligomeric membrane pore formation. Later, we solved PG-2 (PDB ID:2MUH) and PG-3 (PDB ID:2MZ6) structures in the same environment and for PG-3 observed a strong dαα NOE effects between residues R18 and F12, V14, and V16. These “inconsistent” with monomer structure NOEs appears due to formation of an additional antiparallel β-sheet between two monomers. It was also suggested that there is a possible association of protegrins dimers to form octameric or decameric β-barrels in an oligomer state. In order to investigate a more detailed oligomerization process of protegrins, in the present article we report the monomer (PDB ID: 2NC7) and octamer pore structures of the protegrin-5 (PG-5) in the presence of DPC micelles studied by solution NMR spectroscopy. In contrast to PG-1, PG-2, and PG-3 studies, for PG-5 we observed not only dimer NOEs but also several additional NOEs between side chains, which allows us to calculate an octamer pore structure of PG-5 that was in good agreement with previous AFM and PMF data