Search Results - "Doi, Masamitsu"

Quartz crystal microbalance sensor for the detection of collagen model peptides based on the formation of triple helical structure by Fuji, Sota, Tanaka, Kotaro, Kishikawa, Shiho, Morita, Seiichi, Doi, Masamitsu

“…Collagen is a major structural protein, and abnormalities in collagen structure can lead to several connective tissue diseases such as osteoporosis. We report…”
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Conformational preferences of 4-chloroproline residues by Park, Hae Sook, Byun, Byung Jin, Motooka, Daisuke, Kawahara, Kazuki, Doi, Masamitsu, Nakazawa, Takashi, Kobayashi, Yuji, Kang, Young Kee

“…Conformational preferences of the (2S,4R)‐4‐chloroproline (Clp) and (2S,4S)‐4‐chloroproline (clp) residues are explored at the M06‐2X/cc‐pVTZ//M06‐2X/6‐31+G(d)…”
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Different Effects of 4-Hydroxyproline and 4-Fluoroproline on the Stability of Collagen Triple Helix by Nishi, Yoshinori, Uchiyama, Susumu, Doi, Masamitsu, Nishiuchi, Yuji, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji

“…Differential scanning calorimetry (DSC) analyses of a series of collagen model peptides suggest that 4-hydroxyproline (Hyp) and 4-fluoroproline (fPro) have…”
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Simple and efficient syntheses of Boc- and Fmoc-protected 4( R)- and 4( S)-fluoroproline solely from 4( R)-hydroxyproline by Doi, Masamitsu, Nishi, Yoshinori, Kiritoshi, Naruto, Iwata, Tomoya, Nago, Mika, Nakano, Hiroaki, Uchiyama, Susumu, Nakazawa, Takashi, Wakamiya, Tateaki, Kobayashi, Yuji

“…As building blocks of collagen model peptides, Boc- and Fmoc-protected 4( R)- and 4( S)-fluoroproline, which will be widely used in peptide synthesis including…”
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Redox potentials of active-site bis(cysteinyl) fragments of thiol-protein oxidoreductases by Siedler, Frank, Rudolph-Boehner, Sabine, Doi, Masamitsu, Musiol, Hans Juergen, Moroder, Luis

“…The active sites of thiol-protein oxidoreductases consist of the characteristic Cys-X-X-Cys motif, and the redox potentials of these enzymes reflect the…”
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Stabilization mechanism of triple helical structure of collagen molecules by Nishi, Yoshinori, Doi, masamitsu, Uchiyama, Susumu, Nishiuchi, Yuji, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji

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The triple helical structure and stability of collagen model peptide with 4(s)-hydroxyprolyl-pro-gly units by Motooka, Daisuke, Kawahara, Kazuki, Nakamura, Shota, Doi, Masamitsu, Nishi, Yoshinori, Nishiuchi, Yuji, Kang, Young Kee, Nakazawa, Takashi, Uchiyama, Susumu, Yoshida, Takuya, Ohkubo, Tadayasu, Kobayashi, Yuji

“…Extensive studies on the structure of collagen have revealed that the hydroxylation of Pro residues in a variety of model peptides with the typical…”
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Characterization of Collagen Model Peptides Containing 4-Fluoroproline; (4(S)-Fluoroproline-Pro-Gly)10 Forms a Triple Helix, but (4(R)-Fluoroproline-Pro-Gly)10 Does Not by Doi, Masamitsu, Nishi, Yoshinori, Uchiyama, Susumu, Nishiuchi, Yuji, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji

“…Collagen model peptide (Pro-Pro-Gly)10 has a triple helical structure and undergoes a thermal transition to a single random coil structure. The transition…”
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Polymorphism of Collagen Triple Helix Revealed by 19 F NMR of Model Peptide [Pro-4( R )-Hydroxyprolyl-Gly] 3 -[Pro-4( R )-Fluoroprolyl-Gly]-[Pro-4( R )-Hydroxyprolyl-Gly] 3 by Kawahara, Kazuki, Nemoto, Nobuaki, Motooka, Daisuke, Nishi, Yoshinori, Doi, Masamitsu, Uchiyama, Susumu, Nakazawa, Takashi, Nishiuchi, Yuji, Yoshida, Takuya, Ohkubo, Tadayasu, Kobayashi, Yuji

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Polymorphism of Collagen Triple Helix Revealed by 19F NMR of Model Peptide [Pro-4(R)-Hydroxyprolyl-Gly]3-[Pro-4(R)-Fluoroprolyl-Gly]-[Pro-4(R)-Hydroxyprolyl-Gly]3 by Kawahara, Kazuki, Nemoto, Nobuaki, Motooka, Daisuke, Nishi, Yoshinori, Doi, Masamitsu, Uchiyama, Susumu, Nakazawa, Takashi, Nishiuchi, Yuji, Yoshida, Takuya, Ohkubo, Tadayasu, Kobayashi, Yuji

“…We have characterized various structures of (Pro-Hyp R -Gly)3-Pro-fPro R -Gly-(Pro-Hyp R -Gly)3 in the process of cis–trans isomerization and helix–coil…”
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Polymorphism of Collagen Triple Helix Revealed by super(19)F NMR of Model Peptide [Pro-4(R)-Hydroxyprolyl-Gly] sub(3)-[Pro-4(R)-Fluo roprolyl-Gly]-[Pro-4(R)-Hydroxyprolyl-Gly] sub(3) by Kawahara, Kazuki, Nemoto, Nobuaki, Motooka, Daisuke, Nishi, Yoshinori, Doi, Masamitsu, Uchiyama, Susumu, Nakazawa, Takashi, Nishiuchi, Yuji, Yoshida, Takuya, Ohkubo, Tadayasu, Kobayashi, Yuji

“…We have characterized various structures of (Pro-Hyp super(R)-Gly) sub(3)-P ro-fPro super(R)-Gly-(Pro-Hyp super(R)-Gly) sub(3) in the process of cis-trans…”
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Stabilization mechanism of triple helical structure of collagen molecules by Nishi, Yoshinori, Doi, Masamitsu, Doi susumu uchiyama, Masamitsu, Nishiuchi, Yuji, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji

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Conformational analysis of elcatonin in solution by OGAWA, Kiyoshi, NISHIMURA, Shigenori, DOI, Masamitsu, KYOGOKU, Yoshimasa, HAYASHI, Mitsuo, KOBAYASHI, Yuji

“…The conformational characteristics of elcatonin, an analogue of eel calcitonin having a disulfide bond Cys1‐Cys7 replaced by an ethylene linkage between…”
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Collagen-like triple helix formation of synthetic (Pro-Pro-Gly)10 analogues: (4(S)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10, (4(R)-hydroxyprolyl-4(R)-hydroxyprolyl-Gly)10 and (4(S)-fluoroprolyl-4(R)-fluoroprolyl-Gly)10 by Doi, Masamitsu, Nishi, Yoshinori, Uchiyama, Susumu, Nishiuchi, Yuji, Nishio, Hideki, Nakazawa, Takashi, Ohkubo, Tadayasu, Kobayashi, Yuji

“…For the rational design of a stable collagen triple helix according to the conventional rule that the pyrrolidine puckerings of Pro, 4‐hydroxyproline (Hyp) and…”
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Proton NMR study of helical structures initiated by an .alpha.-aminoisobutyric acid residue in oligoleucines by Isokawa, Shizuko, Doi, Masamitsu, Wakita, Ryuhei, Sugasawa, Hiroki, Asakura, Tetsuo, Narita, Mitsuaki

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Molecular structure of Aib-containing oligopeptides, Boc-(Leu3-Aib)2-OBzl and Boc-(Leu3-Aib)3-OBzl by OKUYAMA, K, NAKANISHI, S, DOI, M, NARITA, M, IMADA, K

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Conformational analysis of human calcitonin in solution by Ogawa, Kiyoshi, Nishimura, Shigenori, Doi, Masamitsu, Takashima, Hiroyuki, Nishi, Yoshinori, Yoshida, Takuya, Ohkubo, Tadayasu, Kobayashi, Yuji

“…The solution conformation of human calcitonin in a mixture of 60% water and 40% trifluoroethanol has been determined by the combined use of 1H NMR spectroscopy…”
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Differential effects of fibronectin-derived oligopeptides on the attachment of rabbit lens epithelial cells in vitro by Sasabe, T, Suwa, Y, Kiritoshi, A, Doi, M, Yuasa, T, Kishida, K

“…Among the Arg-Gly-Asp (RGD)-containing sequences that are known to be cell-binding domains of fibronectin, 500 migrograms/ml of Arg-Gly-Asp-Ser (RGDS) and…”
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Solution structure of a human calcitonin analog elucidated by NMR and distance geometry calculations by Katahira, R, Doi, M, Kyogoku, Y, Yamada-Nosaka, A, Yamasaki, K, Takai, M, Kobayashi, Y

“…Three-dimensional structure of a human calcitonin analog (abbreviated as hCTa) in which the amino acids of the wild type are replaced at position 12, 16 and 19…”
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Synthesis and solubility properties of peptide fragments of human hemoglobin alpha-chain (123-136) by Narita, M, Doi, M, Nakai, T, Takegahara, H

“…The solubility prediction method for protected peptides was successfully applied to relatively small peptide fragments of human hemoglobin alpha-chain…”
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