PMC

a Twisting and folding process of the magneto-origami square–twist that is magnetized at the folded state. b Diagonal length δ of magneto-origami square–twist during the folding process. c The unfolding process of the magneto-origami starshade that is magnetized in the flat state. The red marker indicates the movement of a marginal point during the deployment process. The blue sign indicates a magnetization pointing outward. d The diagonal length δ of the magneto-origami starshade during the deployment process.

(a) Machines used for fabrication (b) Layout of fabrics cut using a laser cutter (c) Fabrication procedure of internal TPU bladder (d) Fabrication procedure of knit stretch FRTA for bending. (e) Fabrication procedure of knit Stretch FRTA for twisting and extending. (f) Fabrication procedure for woven fabric actuators. (g) Microscope view and illustration of the yarns in the woven fabric. (h) Microscope view and illustration of the yarns in the knit stretch fabric.

Na⁺-induced twisting in helicate 52. Reprinted with permission from ref (). Copyright 2010 Nature Publishing Group.

Structural changes in the eight-stranded central β-sheet of kinesin. Side (a) and end (b) views of the kinesin β-sheet after a nucleotide-bound structure (1BG2; Kull et al. ) was aligned with a rigor-like structure (4OZQ; Arora et al. ) using the main chain atoms of the P-loop. Mg²⁺ and ADP are shown as space-fill model and are colored magenta and cyan, respectively. c The root-mean-square deviation (RMSD) of complementary residues is plotted for each individual β-strand. d Individual β-strand curvature based on the sum of sequential C_α distances for each β-strand residue (i = initial residue, i + x = final residue) divided by the total distance from initial to final plotted for nucleotide-bound and rigor-like structures. e β-strand torsion angles (τ) relative to β1 are plotted to quantify the degree of twisting within the entire β-sheet. Torsion angles were calculated using the following equation for each individual β-strand: , where are the unit vectors for each respective β-strand (Cecchini et al. ). f The change in each individual β-strand torsion angle (Δτ) as the kinesin central β-sheet transitions from nucleotide-bound (1BG2) to rigor-like (4OZQ) states