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Philosophical Transactions of the Royal Society B: Biological Sciences logoLink to Philosophical Transactions of the Royal Society B: Biological Sciences
. 2004 Dec 29;359(1452):1883–1893. doi: 10.1098/rstb.2004.1557

X-ray diffraction studies of the contractile mechanism in single muscle fibres.

Vincenzo Lombardi 1, Gabriella Piazzesi 1, Massimo Reconditi 1, Marco Linari 1, Leonardo Lucii 1, Alex Stewart 1, Yin-Biao Sun 1, Peter Boesecke 1, Theyencheri Narayanan 1, Tom Irving 1, Malcolm Irving 1
PMCID: PMC1693470  PMID: 15647164

Abstract

The molecular mechanism of muscle contraction was investigated in intact muscle fibres by X-ray diffraction. Changes in the intensities of the axial X-ray reflections produced by imposing rapid changes in fibre length establish the average conformation of the myosin heads during active isometric contraction, and show that the heads tilt during the elastic response to a change in fibre length and during the elementary force generating process: the working stroke. X-ray interference between the two arrays of myosin heads in each filament allows the axial motions of the heads following a sudden drop in force from the isometric level to be measured in situ with unprecedented precision. At low load, the average working stroke is 12 nm, which is consistent with crystallographic studies. The working stroke is smaller and slower at a higher load. The compliance of the actin and myosin filaments was also determined from the change in the axial spacings of the X-ray reflections following a force step, and shown to be responsible for most of the sarcomere compliance. The mechanical properties of the sarcomere depend on both the motor actions of the myosin heads and the compliance of the myosin and actin filaments.

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Selected References

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