Procollagen molecules have amino-terminal and carboxy-terminal propeptides at the respective ends of the collagenous triple helix. The carboxy-terminal propeptides enhance and direct the association of proα-chains into procollagen molecules, but the mechanism of this registration function is still obscure. A hypothesis concerning the function of disulfide bonding in the assembly of types I, II and III procollagen is put forward here. © 1987.
Koivu, J. (1987). Disulfide bonding as a determinant of the molecular composition of types I, II and III procollagen. FEBS Letters, 217(2), 216–220. https://doi.org/10.1016/0014-5793(87)80666-X