Domain-Domain Interactions in Filamin A (16-23) Impose a Hierarchy of Unfolding Forces. Xu, T., Lannon, H., Wolf, S., Nakamura, F., & Brujic, J. BIOPHYSICAL JOURNAL, 104(9):2022-2030, CELL PRESS, 5, 2013. abstract bibtex The quaternary structure of Filamin A (FLNa) 16-23 was recently shown to
exhibit multiple domain-domain interactions that lead to a
propeller-like construction. Here we present single-molecule force
spectroscopy experiments to show a wide variety of mechanical responses
of this molecule and compare it with its linear counterpart FLNa 1-8.
The compact structure of FLNa 16-23 leads to a broad distribution of
rupture forces and end-to-end lengths in the force-extension mode and
multiple unraveling timescales in the force-clamp mode. Moreover, a
subset of force-extension trajectories reveals a mechanical hierarchy in
which the rupture of domain-domain interactions at high forces (>200 pN)
liberates the unfolding of individual domains at low forces (similar to
100 pN). This mechanism may also explain the order-of-magnitude
difference in the rates of the biexponential fits to the distribution of
unfolding dwell times under force-clamp. Overall, FLNa 16-23 under a
force of 100 pN is more compliant than the linear FLNa 1-8. Because a
physiological role of FLNa is to crosslink actin filaments, this range
of responses allows it to accommodate a broad spectrum of forces exerted
by the cell and its environment.
@article{
title = {Domain-Domain Interactions in Filamin A (16-23) Impose a Hierarchy of Unfolding Forces},
type = {article},
year = {2013},
identifiers = {[object Object]},
pages = {2022-2030},
volume = {104},
month = {5},
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city = {600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA},
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abstract = {The quaternary structure of Filamin A (FLNa) 16-23 was recently shown to
exhibit multiple domain-domain interactions that lead to a
propeller-like construction. Here we present single-molecule force
spectroscopy experiments to show a wide variety of mechanical responses
of this molecule and compare it with its linear counterpart FLNa 1-8.
The compact structure of FLNa 16-23 leads to a broad distribution of
rupture forces and end-to-end lengths in the force-extension mode and
multiple unraveling timescales in the force-clamp mode. Moreover, a
subset of force-extension trajectories reveals a mechanical hierarchy in
which the rupture of domain-domain interactions at high forces (>200 pN)
liberates the unfolding of individual domains at low forces (similar to
100 pN). This mechanism may also explain the order-of-magnitude
difference in the rates of the biexponential fits to the distribution of
unfolding dwell times under force-clamp. Overall, FLNa 16-23 under a
force of 100 pN is more compliant than the linear FLNa 1-8. Because a
physiological role of FLNa is to crosslink actin filaments, this range
of responses allows it to accommodate a broad spectrum of forces exerted
by the cell and its environment.},
bibtype = {article},
author = {Xu, Tianyou and Lannon, Herbert and Wolf, Sebastein and Nakamura, Fumihiko and Brujic, Jasna},
journal = {BIOPHYSICAL JOURNAL},
number = {9}
}
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