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- W2904175311 abstract "X-Ray diffraction studies have been made of several polytripeptides related to collagen. The structure of poly(L-prolyl-glycyl-glycine) has been found to consist of helices which resemble the individual strands of the triple helix models for collagen. However, the helices are not coiled about each other as in the collagen models. Both poly(L-prolyl-L-alanyl-glycine) and poly(L-prolyl-glycyl-o-acetyl-L-hydroxyproline) give X-ray patterns which resemble that of collagen, including the characteristic 2·9 Å spacing, but are too diffuse for detailed analysis. Poly (L-prolyl-glycyl-L-proline), however, gives an X-ray pattern which has all the main features of the collagen pattern and is appreciably sharper in detail. As in collagen, water absorption leads to an increase in the equatorial, but not in the meridional, spacings. The X-ray pattern and the density indicate a helical structure for (Pro.Gly.Pro)n with an axial translation of 2·85 Å and a rotation of approximately 108° per tripeptide. Only a structure consisting of three strands coiled about a common axis can be fitted satisfactorily to these helical parameters. Of the three-stranded models that have been proposed for collagen, that with two hydrogen bonds per tripeptide can be excluded on chemical grounds, whereas the collagen I model is incompatible with the observed unit cell. However, slightly modified versions of collagen II or the closely similar alternative Madras structure satisfy both criteria. The results show that neither hydroxy-proline nor more than one interchain hydrogen bond per tripeptide is required for the formation of a collagen-like structure. In the light of recent findings concerning the sequence and other properties of collagen, it is suggested that much of the protein may have a structure very similar to that of (Pro. Gly.Pro)n." @default.
- W2904175311 created "2018-12-22" @default.
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- W2904175311 date "1966-04-01" @default.
- W2904175311 modified "2023-09-23" @default.
- W2904175311 title "Polymers of tripeptides as collagen models" @default.
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- W2904175311 doi "https://doi.org/10.1016/s0022-2836(66)80182-1" @default.
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