The secondary structure of a conserved non-collagenous module in alpha
(V), alpha 1(XI), alpha 1(IX), alpha 1(XII), alpha 1(XIV) and alpha 1(
XVI) collagen chains and in proline- and arginine-rich protein was ana
lyzed using different algorithms. The results predict that a common an
ti-parallel beta-sheet structure composed of nine consensus beta-stran
ds is present in these non-collagenous modules. A model for the packin
g of these beta-sheets is proposed which suggests that the predicted b
eta-sheet structure may be involved in molecular recognition functions
.