Studies on the structure of collagen: I. The sequence analysis of peptides released by pronase
β Scribed by J. Rosmus; Z. Deyl; M.P. Drake
- Book ID
- 115747891
- Publisher
- Elsevier Science
- Year
- 1967
- Weight
- 430 KB
- Volume
- 140
- Category
- Article
- ISSN
- 0005-2795
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π SIMILAR VOLUMES
The amino acid sequence of the collagen al(1) chain (cal0 is analyzed. Deviations of random tripeptide distribution leads to the definition of clusters. Inside these regions, collagen-typical tripeptides are located. Besides Gly-Pro-Hyp, Gly-PreAla, and Gly-Ala-Hyp, the polar sequences Gly-Glu-Hyp,
## Abstract As model peptides of collagen, (ProβProβGly)~__n__~ (__n__ = 10, 12, 14, and 15) and (ProβProβGly)~__n__~(AlaβProβGly)~__m__~(ProβProβGly)~__n__~ (2__n__ + __m__ = 15; __m__ = 1, 3, and 5) were synthesized by the solidβphase method. The final products were pure when checked by highβvolt