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The tendency of collagen molecules to form macromolecular aggregates is well-known. This tendency is common with most fibrous proteins that form filaments with helical symmetry and which occupy equivalent or quasiequivalent positions.

The exact mode in which the collagen molecules pack into microfibrils (precursors of the larger fibrils) still remains a subject for speculation. A five-stranded microfibril was first suggested to account for such a substructure, one that would satisfy the condition that adjacent molecules were quivalently related by a quarterstagger.

When monomeric collagen is heated to 37°C it progressively polymerizes, generating a turbidity curve that reflects the presence of intermediate aggregates. The lag phase (persistence of monomers), the nucleation and appearance of turbidity (microfibrils), and the rapid increase in turbidity (fiber formation) have been equated to how the cell may handle this process.

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