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Folding of a three–stranded coiled coil

Coiled coils consist of two or more amphipathic α–helices wrapped around each other to form a superhelical structure stabi–lized at the interhelical interface by hydrophobic residues spaced in a repeating 3–4 sequence pattern. Dimeric coiled coils have been shown to often form in a single step reaction in which asso–ciation and folding of peptide chains are tightly coupled. Here, we ask whether such a simple folding mechanism may also apply to the formation of a three–stranded coiled coil. The designed 29–residue peptide LZ16A was shown previously to be in a concen–tration–dependent equilibrium between unfolded monomer (M), folded dimer (D), and folded trimer (T). We show by time–resolved fluorescence change experiments that folding of LZ16A to D and T can be described by