Fessler J H, Doege K J, Duncan K G, Fessler L I
J Cell Biochem. 1985;28(1):31-7. doi: 10.1002/jcb.240280106.
During the biosynthesis and assembly of collagen structures, disulfide links can serve several functions. During biosynthesis they successively stabilize intrapeptide folding and associations of three chains into one molecule. Studies on the refolding and reassociation of reduced and denatured carboxyl propeptides of procollagen I showed that successive interactions of folding and assembly are successively weaker. Disulfide bridges were reestablished within correctly refolded carboxyl propeptides. Rearrangements of disulfide bridges may occur during the processing of type V procollagen molecules as these collagens become incorporated into extracellular matrix. The basement membrane procollagen IV molecules become disulfide linked at each end into networks, and there are indications that further rearrangements of disulfide links may allow additional modulation.
在胶原蛋白结构的生物合成和组装过程中，二硫键可发挥多种功能。在生物合成过程中，它们依次稳定肽内折叠以及三条链聚合成一个分子的过程。对原胶原蛋白I还原和变性的羧基前肽的重折叠和重新缔合研究表明，折叠和组装的连续相互作用依次减弱。在正确重折叠的羧基前肽内重新建立了二硫桥。在V型原胶原分子加工过程中，随着这些胶原蛋白整合到细胞外基质中，二硫桥可能会发生重排。基底膜原胶原IV分子在两端通过二硫键连接成网络，并且有迹象表明二硫键的进一步重排可能会带来更多调节作用。
