A Collagen IV NC1 hexamer is a six-subunit junction formed when the C-terminus ends of two Collagen IV protomers associate. Each three-chain protomer contributes three Collagen IV NC1 domains. The resulting arrangement is therefore two three-subunit ends joined together, one local connection in a basement membrane scaffold.[ref]
A Sulfilimine Bond Identified in Collagen IV by Roberto Vanacore and others. Introduction and Figure 3; trimeric ends and six-subunit junction
Up to six sulfilimine bonds can reinforce the interface between the two ends. Analysis of linked peptides by mass spectrometry and nuclear magnetic resonance, followed by chemical reduction that separated the linked components, established the chemistry of this reinforcement.[ref]
A Sulfilimine Bond Identified in Collagen IV by Roberto Vanacore and others. Table 1 and Figures 1–3; crosslinked peptides, bond identification and reduction
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