Triple-Helical Structure of Collagen Based on Single-Crystal Analyses of Model Peptides.

• OKUYAMA Kenji

  東京農工大学工学部 生命工学科

Bibliographic Information

Other Title

• モデルペプチドを用いたコラーゲンの構造研究
• カイセツ モデル ペプチド オ モチイタ コラーゲン ノ コウゾウ ケンキュウ

Abstract

Recent structure analyses of collagen-model peptides revealed several important structural features of collagen. (1) Contrary to the Rich and Crick 10/3-helix, the 7/2-helical conformation is preferable as a structure of collagen. (2) The triple-helical structure is stabilized by a repetitive X (C=O) --- HN (Gly) hydrogen bonds. If X is not Pro or Hyp, the water-bridge, Gly (C=O) --- H₂O --- HN (X), also stabilize the triple-helical structure. (3) The stabilization of collagen by Hyp can be attributed to the inductive effect of the hydroxyl moiety attached to the Cγ of Pro.

Journal

• Nihon Kessho Gakkaishi

  Nihon Kessho Gakkaishi 42 (4), 346-353, 2000

  The Crystallographic Society of Japan

Details

• CRID: 1390001204087591296
• NII Article ID: 10004673708
• NII Book ID: AN00188364
• DOI: 10.5940/jcrsj.42.346
• ISSN: 18845576
• ISSN: 03694585
• NDL BIB ID: 5466836
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5466836
• Text Lang: ja
• Data Source:
  • JaLC
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed