Review Article
Comparative Biomechanics of Thick Filaments and Thin Filaments with Functional Consequences for Muscle Contraction
Table 2
Range of persistence length for biological polymers and nanotubes.
| Material | Persistence Length (m) | Comments and References |
| Silk | 0.0004 | Recombinant spider dragline silk nanofibers [132] | Titin | 0.0007–0.04 | For intact (rabbit skeletal) protein, individual domains, and elastic and inelastic regions [133–135] | Hyaluronan | 0.0045 | Articular cartilage [136] | Collagen | 0.0112–0.057 | Types I, II, III [136, 137] | Projectin | 0.030 | Lethocerus flight muscle [138] | Mucins | 0.036 | Human ocular [139] | Kettin | 0.045 | Recombinant fragments [138] | DNA | 0.053 | 3000 bp [140] | Intermediate filaments | 1 | In vitro polymerized human vimentin [77] | Cofilactin | 2.2 | In vitro polymerized [92] | Actin | 9.0–17.7 | In vitro polymerized with or without phalloidin [10, 12, 92, 141] | Nanotubes | 17–32 | Single walled carbon nanotubes [142] | Flagellar filaments | 2.4–41.1 | From bacteria [129] | Thin filaments | 44–121 | See Table 1 | Thick filaments | 27–1742 | From various species and muscle types [8, 9, 71] | Microtubules | 110–5200 | In vitro polymerized with taxol or paclitaxel [12, 141, 143] |
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