Abstract
Many proteins are known to serve roles as structural scaffolds in cells and tissues. These proteins maintain the shape of the cell, act as local force sensors, and are essential to form tissues that are exposed to large external forces. Although seemingly passive elements, these structural proteins have unique physical features that are worthy of a closer look. In particular, it is critically important to understand how scaffolding proteins and protein complexes respond to the high external forces commonly encountered in biology. In this issue of PNAS, Bertz et al. (1) report a remarkable new feature of these load-bearing complexes. Apparently, evolution has molded these proteins to be remarkably resistant to unfolding when pulled in the same direction as they would experience in the cell. However, in other pulling directions the complex is relatively fragile.
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