| Value |
17
µm
Range: ±2 Table - link µm
|
| Organism |
Generic |
| Reference |
van Mameren J, Vermeulen KC, Gittes F, Schmidt CF. Leveraging single protein polymers to measure flexural rigidity. J Phys Chem B. 2009 Mar 26 113(12):3837-44. p. 3840 right column 3rd paragraph and p.3842 table 1PubMed ID19673071
|
| Method |
"[Researchers] report a new approach to obtain the flexural rigidity
by means of well-controlled active experiments using optical
tweezers to bend the filaments locally, as schematically depicted
in Figure 1. In this way force-extension curves were measured
for taxol-stabilized microtubules and rhodamine-phalloidin labeled
actin filaments." |
| Comments |
"The persistence length Lp is the
exponential decay constant of the thermal tangent-tangent
correlation function along the chain, modeled as a homogeneous
bendable filament and depends on the flexural rigidity EI of
the filament and the temperature T as Lp=EI/kT, where k is
the Boltzmann constant." "The average value found for the flexural
rigidity of actin is EI=(7.1±0.8)×10^-26nm^2 (standard
error of the mean, BNID 105504). This corresponds to a persistence length Lp
for actin of 17±2µm using Lp=EI/kBT [Howard, J. Mechanics of motor proteins and the cytoskeleton
Sinauer Associates: Sunderland, MA, 2001]." Value in range is standard
error of the mean. See BNID 106830 |
| Entered by |
Uri M |
| ID |
105505 |