Bundling of F-actin
Abstract
The ubiquitous protein actin is essential for cell motility and cell structure. F-actin (filamentous actin), a double-stranded helical biopolymer composed of actin monomers, is highly negatively charged. Although F-actin chains repel each other, they can self-assemble into bundles of densely-packed nearly parallel chains in the presence of "linkers" such as multivalent cationic species or actin binding proteins. We use multi-angle static light scattering measurements of F-actin and bundles of F-actin in solution to study the kinetics of bundle formation induced by tetravalent spermine. We find that the data are well-described by a model of non-interacting solid cylinders. By fitting to this model, we extract the bundle diameter as a function of time to gain insight into the kinetics of the bundling process.
- Publication:
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APS March Meeting Abstracts
- Pub Date:
- March 2002
- Bibcode:
- 2002APS..MARF30008S