~10 to 17 μm
||D.N. Robinson, Y.-S. Kee, T. Luo and A. Surcel, Understanding How Dividing Cells Change Shape. In: Edward
H. Egelman, editor: Comprehensive Biophysics, Vol 7, Cell Biophysics, Denis Wirtz. Oxford: Academic Press, 2012.
pp. 48-72. p.54 right column bottom paragraph
||Isambert, H. Venier, P. Maggs, A. C. Fattoum, A. Kassab, R. Pantaloni, D. Carlier, M. F. Flexibility of actin filaments derived from thermal fluctuations. Effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 1995, 270, 11437–11444.PubMed ID7744781
||(Primary source abstract:) "Single actin filaments undergoing brownian movement in two dimensions were observed at 20 degrees C in fluorescence optical video microscopy."
||"The persistence length (Lp) of
a semiflexible polymer can be thought of as the minimum
length between two points on the polymer where the two
points become independent of one another. For actin, the Lp is
~10–17µm (primary source)."