Thermal Stability and Folding of Collagen Triple Helices
スポンサーリンク
概要
- 論文の詳細を見る
There are more than 40 proteins in the collagen super family and they play crucial roles in the whole body. The basic structure of collagens is relatively simple, however, our understanding is still limited and far from a complete understanding of its biological roles. Recent advances in the biophysical characterization of synthetic peptides enhanced our understanding of the structure of the collagen triple helix. In this review, we summarize the recent studies on thermal stability and folding of collagen triple helices and identify the problems that have to be solved in order to further our understanding ofcollagen. The synthetic collagen-like peptides are good tools for making connections between the biophysical and biological studies of collagen.
- 日本結合組織学会の論文
- 2003-12-25
著者
-
Mizuno Kazunori
Shriners Hospital
-
Mizuno Kazunori
Shriners Hospital For Children Research Department And Department Of Biochemistry And Molecular Biol
-
BACHINGER Hans
Shriners Hospital
-
Baechinger Hans
Shriners Hospital For Children Research Department And Department Of Biochemistry And Molecular Biol
関連論文
- Intercellular Accumulation of Type V Collagen Fibrils in Accordance with Cell Aggregation
- Preferential Liberation of Type V Collagen from Bovine Corneal Stroma by Limited Treatment with Proteases
- STRUCTURAL ROLE OF 3-HYDROXYPROLINE IN COLLAGEN
- Thermal Stability and Folding of Collagen Triple Helices