منابع مشابه
Elastic lever-arm model for myosin V.
We present a mechanochemical model for myosin V, a two-headed processive motor protein. We derive the properties of a dimer from those of an individual head, which we model both with a four-state cycle (detached; attached with ADP.Pi; attached with ADP; and attached without nucleotide) and alternatively with a five-state cycle (where the powerstroke is not tightly coupled to the phosphate relea...
متن کاملMyosin V passing over Arp2/3 junctions: branching ratio calculated from the elastic lever arm model.
Myosin V is a two-headed processive motor protein that walks in a hand-over-hand fashion along actin filaments. When it encounters a filament branch, formed by the Arp2/3 complex, it can either stay on the straight mother filament, or switch to the daughter filament. We study both probabilities using the elastic lever arm model for myosin V. We calculate the shapes and bending energies of all r...
متن کاملEssential "ankle" in the myosin lever arm.
C ellular motors are fascinating machines that function by undergoing successive conformational changes that require joints in their structure. Where these are located is particularly critical for molecular motors that produce force with relatively rigid lever arms, such as myosins (1). A long-standing paradox in myosin function may finally be understood from structural insights provided by Coh...
متن کاملDirect measurements of the coordination of lever arm swing and the catalytic cycle in myosin V.
Myosins use a conserved structural mechanism to convert the energy from ATP hydrolysis into a large swing of the force-generating lever arm. The precise timing of the lever arm movement with respect to the steps in the actomyosin ATPase cycle has not been determined. We have developed a FRET system in myosin V that uses three donor-acceptor pairs to examine the kinetics of lever arm swing durin...
متن کاملRole of the lever arm in the processive stepping of myosin V.
Myosin V is a two-headed molecular motor that binds six light chains per heavy chain, which creates unusually long lever arms. This motor moves processively along its actin track in discrete 36-nm steps. Our model is that one head of the two-headed myosin V tightly binds to actin and swings its long lever arm through a large angle, providing a stroke. We created single-headed constructs with di...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2005
ISSN: 0006-3495
DOI: 10.1529/biophysj.104.046763