Journal article
Leveraging Single Protein Polymers To Measure Flexural Rigidity
The journal of physical chemistry. B, Vol.113(12), pp.3837-3844
03/26/2009
Handle:
https://hdl.handle.net/2376/115671
PMID: 19673071
Abstract
The micrometer-scale length of some protein polymers allows them to be mechanically manipulated in single-molecule experiments. This provides a direct way to measure persistence length. We have used a double optical trap to elastically deform single microtubules and actin filaments. Axial extensional force was exerted on beads attached laterally to the filaments. Because the attachments are off the line of force, pulling the beads apart couples to local bending of the filament. We present a simple mechanical model for the resulting highly nonlinear elastic response of the dumbbell construct. The flexural rigidities of the microfilaments that were found by fitting the model to the experimentally observed force−distance curves are (7.1 ± 0.8) × 104 pN·nm2 (persistence length L p = 17.2 μm) for F-actin and (6.1 ± 1.3) × 106 pN·nm2 (L p = 1.4 mm) for microtubules.
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Details
- Title
- Leveraging Single Protein Polymers To Measure Flexural Rigidity
- Creators
- Joost van MamerenKaren C VermeulenFred GittesChristoph F Schmidt
- Publication Details
- The journal of physical chemistry. B, Vol.113(12), pp.3837-3844
- Academic Unit
- Physics and Astronomy, Department of
- Publisher
- American Chemical Society
- Identifiers
- 99900547583301842
- Language
- English
- Resource Type
- Journal article