## 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 fold
Self assembly of mixtures of collagen α-chains
✍ Scribed by Julie Glowacki; Jerome Gross
- Book ID
- 113126528
- Publisher
- Elsevier Science
- Year
- 1981
- Weight
- 334 KB
- Volume
- 668
- Category
- Article
- ISSN
- 0005-2795
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## 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
## Abstract The α chains of collagen are synthesized like other proteins by the sequential addition of amino acids beginning at the amino‐terminal end and continuing for over 1000 amino acids. In addition to amino acid assembly, hydroxylation of certain prolyl and lysyl residues is required to comp