Jürgen Schünemann

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Branchiostoma intermediate filament (IF) protein C2 contains a long tail domain consisting of several degenerate repeats which display a heptad repeat pattern. This unique tail sequence is predicted to constitute a long coiled coil domain in C2, which is separated from the rod by a glycine-rich linker L3. The recombinant IF protein C2 shows, in electron(More)
Previously, we cloned two Branchiostoma IF proteins A3 and B2 and demonstrated that both can form heteropolymeric IF based on a coiled coil dimer consisting of one B2 and one A3 polypeptide. In this study we continued in the characterisation of the B2/A3 heterodimer by searching for the sequences that play an important role in the triggering of the B2/A3(More)
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