## Abstract The aggregation of native acid‐soluble collagen (N‐ASC) and of pronase‐treated acid soluble collagen (P‐ASC) was examined in solution under conditions which varied from those of minimum collagen‐collagen interaction to those leading to incipient fiber formation. Molecular weights and we
Self-assembly of collagen
✍ Scribed by Fessler, John H.
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1974
- Tongue
- English
- Weight
- 260 KB
- Volume
- 2
- Category
- Article
- ISSN
- 0091-7419
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✦ Synopsis
Abstract
The structure and self‐assembly of collagen and procollagen molecules are reviewed. The registration peptides of procollagen have specific recognition properties which assure (1) selection of component polypeptide chains and (2) registration of their N‐termini, facilitating orderly folding into a collagen helix. The stability of this helix relative to body temperature is critically altered by post‐ribosomal hydroxylation of proline residues. The registration peptides of procollagen may have additional functions such as preventing intracellular fiber formation.
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