Molecular and Fibrillar Structures of Collagen
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- OKUYAMA Kenji
- Department of Macromolecular Science, Osaka University
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- KAWAGUCHI Tatsuya
- Department of Macromolecular Science, Osaka University
Bibliographic Information
- Other Title
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- コラーゲンの分子構造・高次構造
- コラーゲン ノ ブンシ コウゾウ コウジ コウゾウ
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Description
The triple helix is a specialized protein motif found in all collagens. The molecular conformation of the collagen-helix confers strict amino acid sequence constraints requiring a Glycine at every third position and a high content of imino acid. Although the X-ray diffraction pattern of fibrous collagen has been studied since the 1920s, deficiencies in the diffraction data have prevented efforts to obtain the unique helical model from the fiber diffraction pattern only. On the other hand, during the past 15 years, many single crystal analyses of collagen model peptides provide various important physicochemical information, including average helical symmetry, the presence of hydrogen bond networks, distribution of water molecules, and structural bases of stabilization of a triple helix induced by hydroxyproline.<br>
Journal
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- KOBUNSHI RONBUNSHU
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KOBUNSHI RONBUNSHU 67 (4), 229-247, 2010
The Society of Polymer Science, Japan
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Keywords
Details 詳細情報について
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- CRID
- 1390282681502013312
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- NII Article ID
- 10026213462
- 130004489250
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- NII Book ID
- AN00085011
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- ISSN
- 18815685
- 03862186
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- NDL BIB ID
- 10656437
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- Text Lang
- ja
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- Data Source
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- JaLC
- NDL Search
- Crossref
- CiNii Articles
- KAKEN
- OpenAIRE
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- Abstract License Flag
- Disallowed