Institut Jean le Rond d'Alembert
Centre National de la Recherche Scientifique
Université Pierre et Marie Curie
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Chirality of coiled-coils: elasticity matters
Sébastien Neukirch, Alain Goriely, and Andrew Hausrath
Physical Review Letters, 100 (2008) 038105also selected in the Virtual Journal of Biological Physics Research -- February 1, 2008 Volume 15, Issue 3.
Abstract : Coiled-coils are important protein-protein interaction motifs with high specificity that are used to assemble macromolecular complexes. Their simple geometric organization, consisting of $\alpha$-helices wrapped around each other, confers remarkable mechanical properties. A geometrical and mechanical continuous model taking into account sequence effects and based on the super-helical winding of the constituent helices is introduced and a continuous family of solutions in which the oligomerization interactions are satisfied is derived. From these solutions, geometric and structural properties, such as the chirality and pitch of the coiled-coil and the location of residues, are obtained. The theoretical predictions are compared to X-ray data from the leucine zipper motif.
Key words : chirality, helix, super-helix, force-extension, keratin, collagen
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