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J Biochem. 1998 Dec 1;124(6):1117-23.

Crystal structure analysis of collagen model peptide (Pro-pro-Gly)10.

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Department of Biotechnology and Life Science, Faculty of Technology, Tokyo University of Agriculture and Technology, Naka-cho, Koganei-shi, Tokyo, 184-8588, Japan.


Single crystals of (Pro-Pro-Gly)10 were grown by the hanging drop method. The crystals diffracted to a resolution of 1.8 A. In the crystals the polypeptides form triple helices that aggregate end-to-end mediated by the solvent molecules, with the basic repeat being 20 A along the helical axis. Analysis of the 20 A structure of (Pro-Pro-Gly)10 using data up to a resolution of 1.9 A revealed that the overall structure is in accordance with the 7/2 model proposed for collagen. The three strands are held together by the (Gly) N-H O (Pro-X) hydrogen bond interactions, and additional stability is provided by the (Pro-Y) Calpha -H O (Pro-X) hydrogen bonding interactions.

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