論文

査読有り 国際誌
2012年6月

Polymorphism of Collagen Triple Helix Revealed by F-19 NMR of Model Peptide [Pro-4(R)-Hydroxyprolyl-Gly](3)-[Pro-4(R)-Fluoroprolyl-Gly]-[Pro-4(R)-Hydroxyprolyl-Gly](3)

JOURNAL OF PHYSICAL CHEMISTRY B
  • Kazuki Kawahara
  • Nobuaki Nemoto
  • Daisuke Motooka
  • Yoshinori Nishi
  • Masamitsu Doi
  • Susumu Uchiyama
  • Takashi Nakazawa
  • Yuji Nishiuchi
  • Takuya Yoshida
  • Tadayasu Ohkubo
  • Yuji Kobayashi
  • 全て表示

116
23
開始ページ
6908
終了ページ
6915
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1021/jp212631q
出版者・発行元
AMER CHEMICAL SOC

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 transition by exploiting the sole F-19 NMR probe in 4(R)-fluoroproline (fPro(R)). Around the transition temperature (T-m), we detected a species with a triple helical structure distinct from the ordinary one concerning the alignment of three strands. The F-19-F-19 exchange spectroscopy showed that this misaligned and that the ordinary triple helices were interchangeable only indirectly via an extended monomer strand with all-trans peptide bonds at Pro-fPro(R), Pro-Hyp(R), and Gly-Pro in the central segment. This finding demonstrates that the helix coil transition of collagen peptides is not described with a simple two-state model. We thus elaborated a scheme for the transition mechanism of (Pro-HypR-Gly),, that the most extended monomer strand can be the sole source both to the misaligned and correctly folded triple-helices. The staggered ends could help misaligned triple helices to self-assemble to higher-order structures. We have also discussed the possible relationship between the misaligned triple helix accumulating maximally at T-m and the kinetic hysteresis associated with the helix coil transition of collagen.

リンク情報
DOI
https://doi.org/10.1021/jp212631q
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/22381006
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000305356100036&DestApp=WOS_CPL
ID情報
  • DOI : 10.1021/jp212631q
  • ISSN : 1520-6106
  • eISSN : 1520-5207
  • PubMed ID : 22381006
  • Web of Science ID : WOS:000305356100036

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