TY - JOUR
T1 - Neurofilaments Function as Shock Absorbers
T2 - Compression Response Arising from Disordered Proteins
AU - Kornreich, Micha
AU - Malka-Gibor, Eti
AU - Zuker, Ben
AU - Laser-Azogui, Adi
AU - Beck, Roy
N1 - Publisher Copyright:
© 2016 American Physical Society.
PY - 2016/9/29
Y1 - 2016/9/29
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=84992109609&partnerID=8YFLogxK
U2 - 10.1103/PhysRevLett.117.148101
DO - 10.1103/PhysRevLett.117.148101
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AN - SCOPUS:84992109609
SN - 0031-9007
VL - 117
JO - Physical Review Letters
JF - Physical Review Letters
IS - 14
M1 - 148101
ER -