Výsledky vyhledávání - "Akihiro Aoki"

Lamellar Structure in Alanine–Glycine Copolypeptides Studied by Solid-State NMR Spectroscopy: A Model for the Crystalline Domain of Bombyx mori Silk Fibroin in Silk II Form

Autor: Chie Ito, Ikue Suzuki, Akihiro Aoki, Tetsuo Asakura, Hironori Kaji, Kohei Komatsu, Akira Naito

Publikováno v: Biomacromolecules. 21:3102-3111

Bombyx mori silk fibroin (SF) fibers with excellent mechanical properties have attracted widespread attention as new biomaterials. However, the structural details are still not conclusive. Here, we propose a lamellar structure for the crystalline dom

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1e3f4f0c5a62113b80ad556e5b6ad6aa
https://doi.org/10.1021/acs.biomac.0c00486

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Infrared‐A Irradiation‐induced Inhibition of Human Keratinocyte Proliferation and Potential Mechanisms

Autor: Takuya Takahashi, Syota Shimizu, Akihiro Aoki, Fumiki Harano

Publikováno v: Photochemistry and Photobiology

Infrared‐A (IRA), which can penetrate deeply into the human skin, is a major component of solar radiation and is recognized to promote photoaging of human dermis. To our knowledge, however, the cellular and molecular consequences of human epidermis

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c0b39efbf1d0c0bf28316c4873bf9d38
http://europepmc.org/articles/PMC7586992

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Packing Structure of Antiparallel β-Sheet Polyalanine Region in a Sequential Model Peptide of Nephila clavipes Dragline Silk Studied Using 13C Solid-State NMR and MD Simulation

Autor: Akio Nishimura, Tetsuo Asakura, Akihiro Aoki, Akira Naito

Publikováno v: Biomacromolecules. 20:3884-3894

Packing structures of polyalanine regions, which are considered to be the reason for the extremely high strength of spider dragline silks, were studied using a series of sequential peptides: (Glu)4...

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4ca87ab60ecfd0f39cb46b89357ce762
https://doi.org/10.1021/acs.biomac.9b00969

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Conformational change of 13C-labeled 47-mer model peptides of Nephila clavipes dragline silk in poly(vinyl alcohol) film by stretching studied by 13C solid-state NMR and molecular dynamics simulation

Autor: Akihiro Aoki, Hironori Matsuda, Naomi Kataoka, Tetsuo Asakura, Akiko Imai

Publikováno v: International Journal of Biological Macromolecules. 131:654-665

For determination of the conformation of irregular sequences in glycine-rich region of the Nephila clavipes spider dragline silk, the combination of 13C selectively labeled model peptides for the typical primary structure and their 13C solid-state NM

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::ffe14a5e7a1ed91691e4e643c6b41bec
https://doi.org/10.1016/j.ijbiomac.2019.03.112

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Structural Analyses of Alanine Trimer and Tetramer Crystals with Antiparallel and Parallel β-Sheet Structures Using Solid-State 1H Spin-Diffusion 2D Correlation NMR Spectroscopy

Autor: Tetsuo Asakura, Akira Naito, Shunsuke Kametani, Akihiro Aoki

Publikováno v: The Journal of Physical Chemistry B. 122:9373-9381

Poly-l-alanine (PLA) sequences are key elements of the crystalline domains of spider dragline and wild silkworm silks. In the present work, 1H spin-diffusion two-dimensional (2D) correlation NMR spectra were observed for selectively deuterated (Ala)3

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::56d06f809b046f08e87a0213d23abef2
https://doi.org/10.1021/acs.jpcb.8b07859

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Mixture of Rectangular and Staggered Packing Arrangements of Polyalanine Region in Spider Dragline Silk in Dry and Hydrated States As Revealed by 13C NMR and X-ray Diffraction

Autor: Tetsuo Asakura, Akihiro Aoki, Akio Nishimura, Yugo Tasei

Publikováno v: Macromolecules. 51:1058-1068

For the first time, we determined the relative percentages of “rectangular” and “staggered” packing arrangements in the crystalline polyalanine regions with antiparallel β-sheet structure within spider dragline silk fiber from Nephila clavat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::8504a88b7ec8763470198fdee6611cba
https://doi.org/10.1021/acs.macromol.7b02627

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Refined Crystal Structure of Samia cynthia ricini Silk Fibroin Revealed by Solid-State NMR Investigations

Autor: Akio Nishimura, Furitsu Suzuki, Akira Naito, Tetsuo Asakura, Shunsuke Kametani, Shuto Kawanishi, Hironori Kaji, Akihiro Aoki

Publikováno v: Biomacromolecules. 18:1965-1974

Samia cynthia ricini is one of the wild silkworms and its silk fibroin (SF) consists of alternatively repeating poly-l-alanine (PLA) sequences as crystalline domain and glycine-rich sequences as noncrystalline domain; the structure is similar to thos

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2df39a9fdebc46491a8ddf39f7b7a953
https://doi.org/10.1021/acs.biomac.7b00441

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