HSP47 is a molecular chaperone that plays an unknown role during the assembly and
transport of procollagen. Our previous studies showed that, unlike most chaperones, HSP47
interacts with a correctly folded substrate. We suggested that HSP47 either stabilizes the
correctly folded collagen helix from heat denaturation or prevents lateral aggregation prior to
its transport from the endoplasmic reticulum. In this study we have addressed the role of
triple helix stability in the binding of HSP47 to procollagen by expressing procollagen …