@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},
 publisher = {CELL PRESS},
 city = {600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA},
 id = {a2ea99ab-e2f8-3412-bb55-2f7b5341e0d8},
 created = {2015-12-14T19:51:29.000Z},
 file_attached = {false},
 profile_id = {3187ec9d-0fcc-3ba2-91e0-3075df9b18c3},
 group_id = {d75e47fd-ff52-3a4b-bf1e-6ebc7e454352},
 last_modified = {2017-03-14T12:30:08.401Z},
 read = {false},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {ISI:000318754300023},
 source_type = {article},
 user_context = {Article},
 private_publication = {false},
 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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Here we present single-molecule force\nspectroscopy experiments to show a wide variety of mechanical responses\nof this molecule and compare it with its linear counterpart FLNa 1-8.\nThe compact structure of FLNa 16-23 leads to a broad distribution of\nrupture forces and end-to-end lengths in the force-extension mode and\nmultiple unraveling timescales in the force-clamp mode. Moreover, a\nsubset of force-extension trajectories reveals a mechanical hierarchy in\nwhich the rupture of domain-domain interactions at high forces (>200 pN)\nliberates the unfolding of individual domains at low forces (similar to\n100 pN). This mechanism may also explain the order-of-magnitude\ndifference in the rates of the biexponential fits to the distribution of\nunfolding dwell times under force-clamp. Overall, FLNa 16-23 under a\nforce of 100 pN is more compliant than the linear FLNa 1-8. Because a\nphysiological role of FLNa is to crosslink actin filaments, this range\nof responses allows it to accommodate a broad spectrum of forces exerted\nby 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","bibtex":"@article{\n title = {Domain-Domain Interactions in Filamin A (16-23) Impose a Hierarchy of Unfolding Forces},\n type = {article},\n year = {2013},\n identifiers = {[object Object]},\n pages = {2022-2030},\n volume = {104},\n month = {5},\n publisher = {CELL PRESS},\n city = {600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA},\n id = {a2ea99ab-e2f8-3412-bb55-2f7b5341e0d8},\n created = {2015-12-14T19:51:29.000Z},\n file_attached = {false},\n profile_id = {3187ec9d-0fcc-3ba2-91e0-3075df9b18c3},\n group_id = {d75e47fd-ff52-3a4b-bf1e-6ebc7e454352},\n last_modified = {2017-03-14T12:30:08.401Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n citation_key = {ISI:000318754300023},\n source_type = {article},\n user_context = {Article},\n private_publication = {false},\n abstract = {The quaternary structure of Filamin A (FLNa) 16-23 was recently shown to\nexhibit multiple domain-domain interactions that lead to a\npropeller-like construction. Here we present single-molecule force\nspectroscopy experiments to show a wide variety of mechanical responses\nof this molecule and compare it with its linear counterpart FLNa 1-8.\nThe compact structure of FLNa 16-23 leads to a broad distribution of\nrupture forces and end-to-end lengths in the force-extension mode and\nmultiple unraveling timescales in the force-clamp mode. Moreover, a\nsubset of force-extension trajectories reveals a mechanical hierarchy in\nwhich the rupture of domain-domain interactions at high forces (>200 pN)\nliberates the unfolding of individual domains at low forces (similar to\n100 pN). This mechanism may also explain the order-of-magnitude\ndifference in the rates of the biexponential fits to the distribution of\nunfolding dwell times under force-clamp. Overall, FLNa 16-23 under a\nforce of 100 pN is more compliant than the linear FLNa 1-8. 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