Mechanical unfolding reveals stable 3-helix intermediates in talin and α-catenin
Fig 3
Representative structure snapshots from SMD.
Talin rod domain bundles and α-catenin (MI-MII) in constant velocity SMD simulations. Structures were taken (a) at 0, 5, 10 and 15 ns for monomers, and (b) at 0, 10, 20 and 30 ns for tandem constructs. Cysteine residues forming the disulphide clamps shown as magenta spheres. Unfolded structures are cut away and presented by dashed line with a helix identifier.