1. Structural studies of collagen-like sequential polypeptides
- Author
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Ö Saygin, G Heymer, K Khodadadeh, E.M Sheikh, H.G Neiss, and Eckhart R. Heidemann
- Subjects
Collagen type ,Crystallography ,animal structures ,Aqueous solution ,integumentary system ,Polymers and Plastics ,Chemistry ,Stereochemistry ,embryonic structures ,Organic Chemistry ,Materials Chemistry ,Circular dichroism spectra - Abstract
Sequential polyhexapeptides, synthesised by combination of sequences from collagen type Gly-X-Y (X = Ala, Pro, Ser; Y = Ala, Gly, Lys, Pro), were characterized by the temperature dependence of circular dichroism spectra. Under comparable conditions these studies revealed that alternating triplets of Gly-Pro-Pro or Gly-Pro-Ala combined with Gly-Pro-Lys or Gly-Pro-Glu exhibit collagen-like structures in aqueous solutions. In case of unstructured chains of (Gly-Pro-Ala) ≈ 12 it can be shown that N-terminal crosslinking of three chains produces a similar ordered structure.
- Published
- 1977
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