Strong Binding of Myosin Heads Stretches and Twists the Actin Helix

Strong Binding of Myosin Heads Stretches and Twists the Actin Helix

Calculation of the size of the power stroke of the myosin motor in contracting muscle requires knowledge of the compliance of the myofilaments. Current estimates of actin compliance vary significantly introducing uncertainty in the mechanical parameters of the motor. Using x-ray diffraction on small...

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Veröffentlicht in:Biophysical journal 2005-03, Vol.88 (3), p.1902-1910
Hauptverfasser: Tsaturyan, Andrey K., Koubassova, Natalia, Ferenczi, Michael A., Narayanan, Theyencheri, Roessle, Manfred, Bershitsky, Sergey Y.
Format: Artikel
Sprache:eng
Schlagworte:
Actins - analysis
Actins - chemistry
Animals
Binding Sites
Biophysics
Cells, Cultured
Diffraction
Elasticity
Micromanipulation - methods
Molecular Motor Proteins - chemistry
Muscle and Contractility
Muscle Fibers, Skeletal - chemistry
Muscular system
Myosins - analysis
Myosins - chemistry
Physical Stimulation - methods
Protein Binding
Protein Conformation
Proteins
Psoas Muscles - chemistry
Rats
Rotation
Sarcomeres - chemistry
Stress, Mechanical
X-rays
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Zusammenfassung:Calculation of the size of the power stroke of the myosin motor in contracting muscle requires knowledge of the compliance of the myofilaments. Current estimates of actin compliance vary significantly introducing uncertainty in the mechanical parameters of the motor. Using x-ray diffraction on small bundles of permeabilized fibers from rabbit muscle we show that strong binding of myosin heads changes directly the actin helix. The spacing of the 2.73-nm meridional x-ray reflection increased by 0.22% when relaxed fibers were put into low-tension rigor (
ISSN:0006-3495
1542-0086
DOI:10.1529/biophysj.104.050047