Výsledky vyhledávání - "Shin-ichi Segawa"

NMR Analysis of a Kinetically Trapped Intermediate of a Disulfide-Deficient Mutant of the Starch-Binding Domain of Glucoamylase

Autor: Hayuki Sugimoto, Yasuo Noda, Shin-ichi Segawa

Publikováno v: Journal of Molecular Biology. 412:304-315

A thermally unfolded disulfide-deficient mutant of the starch-binding domain of glucoamylase refolds into a kinetically trapped metastable intermediate when subjected to a rapid lowering of temperature. We attempted to characterise this intermediate

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c85a98771cab8847fc7bac776c03340
https://doi.org/10.1016/j.jmb.2011.07.025

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The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: Difference in helix propensity of two synthetic peptides with single amino acid substitution

Autor: Satoshi Iimura, Yasuo Noda, Shin-ichi Segawa, Katsuhide Yutani, Taro Umezaki

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 71:737-742

In the denatured state (D1 state) of cystein-free pyrrolidone carboxyl peptidase (PCP-0SH) from Pyrococcus furiosus, a hyperthermophile under nondenaturing conditions, a fairly stable α-helix (α6-helix) has been determined from H/D exchange-NMR exp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1eb5cf8b1ed3ca833077020e55d64ca
https://doi.org/10.1002/prot.21742

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Characterization of the Denatured Structure of Pyrrolidone Carboxyl Peptidase from a Hyperthermophile under Nondenaturing Conditions: Role of the C-Terminal α-Helix of the Protein in Folding and Stability

Autor: Hiromasa Yagi, Katsuhide Yutani, Makoto Takeuchi, Kyoko Ogasahara, Yasuo Noda, Shin-ichi Segawa, Taro Umezaki, Satoshi Iimura, Mineyuki Mizuguchi, Hideo Akutsu

Publikováno v: Biochemistry. 46:3664-3672

The cysteine-free pyrrolidone carboxyl peptidase (PCP-0SH) from a hyperthermophile, Pyrococcus furiosus, can be trapped in the denatured state under nondenaturing conditions, corresponding to the denatured structure that exists in equilibrium with th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::61454898ff271ce9f0fa55ff9f285f29
https://doi.org/10.1021/bi602456y

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A Hydrogen-Exchange NMR Study of Structural Fluctuations of Protein

Autor: Satoshi Iimura, Yasuo Noda, Shin-ichi Segawa

Publikováno v: Journal of the Spectroscopical Society of Japan. 55:379-387

The NMR structure determination method is well established as a powerful tool in protein research, but an amide hydrogen-exchange NMR is also a unique approach, providing important information on structural fluctua-tions in protein at the resolution

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::92fe610dd8422c9aec8c5cd84099f671
https://doi.org/10.5111/bunkou.55.379

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Characterisation of Disulfide-Bond Dynamics in Non-Native States of Lysozyme and Its Disulfide Deletion Mutants by NMR

Autor: Harald Schwalbe, Shin-ichi Segawa, Christopher M. Dobson, Hideki Tachibana, Kenichi Hirai, Emily S. Collins, Julia Wirmer

Publikováno v: ChemBioChem. 6:1619-1627

This report describes NMR-spectroscopic investigations of the conformational dynamics of disulfide bonds in hen-egg-white lysozyme substitution mutants. The following four systems have been investigated: 2SS(alpha), a lysozyme variant that contains C

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebe151b90e7f1851ed90afee629c6471
https://doi.org/10.1002/cbic.200500196

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NMR Structural Study of Two-Disulfide Variant of Hen Lysozyme: 2SS[6−127, 30−115]A Disulfide Intermediate with a Partly Unfolded Structure

Autor: Takeshi Tominaga, Atsushi Yokota, Hideki Tachibana, Daisuke Horii, Yasuo Noda, Shin-ichi Segawa, Yoshiaki Tanisaka

Publikováno v: Biochemistry. 41:2130-2139

The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51d2bd2960dcdaeac7942672211a934f
https://doi.org/10.1021/bi0113418

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The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridge

Autor: Yukiko Kubo, Yasuo Noda, Shin-ichi Segawa, Hideki Tachibana, Yasuko Koumoto, Masanori Takai, Kazuki Izutani, Atsushi Yokota

Publikováno v: Journal of Molecular Biology. 295:1275-1288

The effects of lacking a specific disulfide bridge on the transition state in folding were examined in order to explore the folding-unfolding mechanism of lysozyme. Four species of three-disulfide variant of hen lysozyme (3SS-lysozyme) were prepared

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11a22c695630f046515d27a09f4d142e
https://doi.org/10.1006/jmbi.1999.3442

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