Figure 1: Design of double-cysteine mutants of the 380-kDa dynein motor domain for disulfide cross-linking between the two helices of the stalk coiled coil. These studies, especially the helix-sliding ...

A statistical mechanical theory on the effects of denaturant on the helix–coil transition of polypeptides was developed. In the proposed theory, unfolding agents were assumed to interact with the ...

The biological functions of coiled coils generally depend on efficient folding and perfect pairing of their α-helices. Dynamic changes in the helical registry that lead to staggered helices have only ...

Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between α-helices in a classical coiled coil is formed by ...