AI Article Synopsis
- Researchers are studying how actin filaments attach to surfaces to observe the movements of proteins like tropomyosin, which wraps around actin.
- Two different ways actin can be attached to surfaces are being tested: attached at multiple points along its length or anchored at one end and aligned by fluid flow.
- A new software tool has been developed to help analyze the interactions and movements of these proteins in fluorescent images, revealing similar behavior of tropomyosin regardless of the attachment method.
Article Abstract
Reconstitution of actin filaments on surfaces for observation of filament-associated protein dynamics by fluorescence microscopy is currently an exciting field in biophysics. Here we examine the effects of attaching actin filaments to surfaces on the binding and dissociation kinetics of a fluorescence-labeled tropomyosin, a rod-shaped protein that forms continuous strands wrapping around the actin filament. Two attachment modalities of the actin to the surface are explored: where the actin filament is attached to the surface at multiple points along its length; and where the actin filament is attached at one end and aligned parallel to the surface by buffer flow. To facilitate analysis of actin-binding protein dynamics, we have developed a software tool for the viewing, tracing and analysis of filaments and co-localized species in noisy fluorescence timelapse images. Our analysis shows that the interaction of tropomyosin with actin filaments is similar for both attachment modalities. © 2016 Wiley Periodicals, Inc.
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| http://dx.doi.org/10.1002/cm.21342 | DOI Listing |
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