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| Content Provider | Springer Nature Link |
|---|---|
| Author | Okuyama, Kenji Kamitori, Shigehiro |
| Copyright Year | 1999 |
| Abstract | After about fifty years since the prediction of a triple-helical structure, there are still two models for collagen with different helical symmetry. One is the Rich and Crick model in which three strands form a left-handed 10/3-helix with an axial repeat of 28.6Å. The other is the Okuyama model in which three strands form a left-handed 7/2-helix with an axial repeat of 20Å. High-resolution structures of collagen model peptides (Pro-Pro-Gly)$_{10}$ and (Pro-Hyp-Gly)$_{10}$ strongly support the latter model. The comparison of water molecules found in these structures, together with the water bridges involving the hydroxyl group of Hyp, indicated that water molecules do not contribute to the extra stability of the triple-helix as has been considered for many years. This observation agreed well with a recent finding that the extra stability of collagen with Hyp at the Y-position is due to the inductive effects rather than water bridges involving hydroxyl groups. |
| Starting Page | 19 |
| Ending Page | 34 |
| Page Count | 16 |
| File Format | |
| ISSN | 02534134 |
| Journal | Journal of Chemical Sciences |
| Volume Number | 111 |
| Issue Number | 1 |
| e-ISSN | 09737103 |
| Language | English |
| Publisher | Springer India |
| Publisher Date | 1999-01-01 |
| Publisher Institution | Indian Academy of Sciences |
| Publisher Place | New Delhi |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Collagen model peptide structure of collagen triple helical structure Pro-Pro-Gly Pro-Hyp-Gly stability of triple helix Chemistry/Food Science |
| Content Type | Text |
| Resource Type | Article |
| Subject | Chemistry |
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