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 ...
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 ...
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 ...
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