Procollagen C-linked trimers Collagen propeptides Association of procollagen chains Authored: Jupe, S, 2010-07-20 Edited: Jupe, S, 2012-05-14 Pubmed171650 Pubmed1867713 Pubmed22001560 Pubmed710449 Pubmed710450 Reactome Database ID Release 432002401 Reactome, http://www.reactome.org ReactomeREACT_121254 Reviewed: Canty-Laird, EG, 2012-05-24 The C-propeptides are essential for the association of three alpha chains into a trimeric non-helical procollagen. Alignment determines the composition of the trimer, brings the individual chains into the correct register and initiates formation of the triple helix at the C-terminus, which then proceeds to the N-terminus in a zipper-like fashion (Engel & Prockop 1991). Most early refolding studies were performed with collagen type III which contains a disulfide linkage at the C-terminus of its triple helix (Bächinger et al. 1978, Bruckner et al. 1978) that acts as a permanent linker even after removal of the non-collagenous domains. <br><br>Mutations within the C-propeptides further suggest that they are crucial for the correct interaction of the three polypeptide chains and for subsequent correct folding (refs. in Boudko et al. 2011).