Recent X-ray analyses and synthetic model studies of the coiled-coil motif have clarified roles for hydrophobic core residues and ionic interactions in determining stability, selectivity, stoichiometry and orientation of alpha-helices in this structure. Although much remains to be learnt, current knowledge now enables this motif to be used in novel constructs and points the way to a more explicit understanding of native coiled-coil formation and protein folding in general.
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