- ICS nm -Telramer

Figure 1 Diagrammatic representation of type I (A), IV (B) and VI (C) collagen molecules and their supramolecular arrangements. Triple helical and globular portions not drawn to size. Variation in the size of the triple helical portion of the molecule, and the size and nature of the N- and C-terminal globular ends, determines to a large part the way in which individual monomers can aggregate. Type I collagen forms 67 nm cross-banded fibers/fibrils by quarter-staggered arrays of individual monomers. Type IV collagen forms a flexible open network by association through both the N- and C-terminal ends of the molecule. Type VI collagen with a short triple helix and large globular extensions allows lateral association of two antiparallel monomers and two of these dinners associate in a parallel fashion with their ends in register. End-to-end association of the tetramers forms 105 nm beaded microfibrils

Table 2 Glycosaminoglycans

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