Abstract
What can cells gain by using disordered, rather than folded, proteins in the architecture of their skeleton? Disordered proteins take multiple coexisting conformations, and often contain segments which act as random-walk-shaped polymers. Using x-ray scattering we measure the compression response of disordered protein hydrogels, which are the main stress-responsive component of neuron cells. We find that at high compression their mechanics are dominated by gaslike steric and ionic repulsions. At low compression, specific attractive interactions dominate. This is demonstrated by the considerable hydrogel expansion induced by the truncation of critical short protein segments. Accordingly, the floppy disordered proteins form a weakly cross-bridged hydrogel, and act as shock absorbers that sustain large deformations without failure.
- Received 31 March 2016
DOI:https://doi.org/10.1103/PhysRevLett.117.148101
© 2016 American Physical Society
Physics Subject Headings (PhySH)
Synopsis
Proteins as Shock Absorbers
Published 29 September 2016
Proteins in nerve cells function like shock absorbers that protect the cells from mechanical stress.
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