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• W2037018548 abstract "The amino acid sequence of collagen α1 chain has been compared with itself at various displacements to search for systematic and significant repeats. It shows regularities at intervals related to the stagger between adjacent triple-helical molecules in the fibril, at a distance D of 670 Å or 78 (Gly-X-Y) triplets. The statistically significant similarities are confined to the series X positions of the sequence, especially the hydrophobic amino acids and proline, and show clearly when long sections of sequence of length D are compared. They are of two kinds. (1) Three long regions, separated from one another by 155, 78 and 233 triplets, respectively, show a consistent weak homology, suggesting that the sequence contains three regular D-segments of 78 and a short different segment of 77 triplets. (2) An irregular but highly significant periodic variation in the similarity of the sequence to itself, which shows strong Fourier peaks at wavelengths of D/5, D/6, D/11 and 3D/5. It is proposed that gene duplication of segments of length D, combined with the adaptation of the sequence to guide the molecules into a structure with several periodic types of packing, have produced these effects." @default.
• W2037018548 created "2016-06-24" @default.
• W2037018548 creator A5085061760 @default.
• W2037018548 date "1976-10-01" @default.
• W2037018548 modified "2023-09-27" @default.
• W2037018548 title "Evidence for gene duplication in collagen" @default.
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• W2037018548 doi "https://doi.org/10.1016/s0022-2836(76)80024-1" @default.
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