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Optical trap technique measures single-molecule forces

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The molecular mechanics of the cell are a frontier that scientists still are striving to learn more about. For example, the cell’s cytoskeleton — which provides structural integrity — is of interest to biologists. The structure arises from actin filaments that assemble into networks and bundles, a process regulated by actin-binding proteins. Scientists don’t understand how the molecular interactions between the actin filaments and the proteins that bind to them regulate cytoskeleton properties.

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In the July 8, 2008, issue of PNAS, researchers from MIT in Cambridge, Mass., together with investigators from other institutions, report on a single-molecule method to study the strength of interactions between a single actin-binding protein linking two actin filaments. To do so, they immobilized actin filaments on the surface of a flow channel, then introduced an actin-binding protein. One of the filaments was bound to a bead that was then captured in an optical trap. They moved the sample away from the trap using a piezo stage, until the bond between the actin filaments and the actin-binding protein broke. This provided information on the force required to break the interaction.

The findings from this experiment supported the hypothesis that both unbinding and unfolding play a significant role in regulating the dynamic behavior of the cytoskeleton.
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Published: July 2008
As We Go To PressBiophotonicsBreaking Newscell’s cytoskeletonmolecular mechanicsPresstime Bulletinscientists

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