Motor proteins are force-generating nanomachines that are highly adaptable to their ever-changing biological environments and have a high energy conversion efficiency. Here we constructed an imaging system that uses optical tweezers and a DNA handle to visualize elementary mechanical processes of a nanomachine under load. We apply our system to myosin-V, a well-known motor protein that takes 72 nm 'hand-over-hand' steps composed of a 'lever-arm swing' and a 'Brownian search-and-catch'. We find that the lever-arm swing generates a large proportion of the force at low load (<0.5 pN), resulting in 3 k B T of work. At high load (1.9 pN), however, the contribution of the Brownian search-and-catch increases to dominate, reaching 13 k B T of work. We believe the ability to switch between these two force-generation modes facilitates myosin-V function at high efficiency while operating in a dynamic intracellular environment. © 2012 Macmillan Publishers Limited. All rights reserved.

Switching of myosin-V motion between the lever-arm swing and Brownian search-and-catch

Marcucci L.
Software
;
2012

Abstract

Motor proteins are force-generating nanomachines that are highly adaptable to their ever-changing biological environments and have a high energy conversion efficiency. Here we constructed an imaging system that uses optical tweezers and a DNA handle to visualize elementary mechanical processes of a nanomachine under load. We apply our system to myosin-V, a well-known motor protein that takes 72 nm 'hand-over-hand' steps composed of a 'lever-arm swing' and a 'Brownian search-and-catch'. We find that the lever-arm swing generates a large proportion of the force at low load (<0.5 pN), resulting in 3 k B T of work. At high load (1.9 pN), however, the contribution of the Brownian search-and-catch increases to dominate, reaching 13 k B T of work. We believe the ability to switch between these two force-generation modes facilitates myosin-V function at high efficiency while operating in a dynamic intracellular environment. © 2012 Macmillan Publishers Limited. All rights reserved.
2012
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11577/3332861
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