STRUCTURAL EFFECTS OF CROSS-LINKING REAGENTS ON TRIPLE-HELIX REFORMATION OF INTRAMOLECULARLY CROSS-LINKED COLLAGEN

Intramolecular cross-links were introduced into collagen molecules wit h six kinds of cross-linking reagents at a dilute concentration of pro tein where intermolecular cross-links rarely occurred. Cross-linked co llagen molecules regenerated the triple-helical structure from the hea t-denatured conformation. The cross-links consisting of an aliphatic h ydrocarbon chain were more effective in the regeneration of the collag en structure than the cross-links containing one or two aromatic rings .