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Biosynthesis of collagen
Author(s) -
Fessler John H.,
Doege Kurt J.,
Duncan Keith G.,
Fessler Liselotte I.
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240280106
Subject(s) - procollagen peptidase , disulfide bond , biosynthesis , protein precursor , chemistry , extracellular matrix , folding (dsp implementation) , biochemistry , molecule , peptide , protein folding , extracellular , basement membrane , stereochemistry , biophysics , microbiology and biotechnology , gene , biology , organic chemistry , electrical engineering , engineering
During the biosynthesis and assembly of collagen structures, disulfide links can serve several functions. During biosynthesis they successively stabilize intra‐peptide 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.