Disulfide bonding as a determinant of the molecular composition of types I, II and III procollagen

Abstract

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.