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
- 巻
- 116
- 号
- 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
- ID情報
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- DOI : 10.1021/jp212631q
- ISSN : 1520-6106
- eISSN : 1520-5207
- PubMed ID : 22381006
- Web of Science ID : WOS:000305356100036