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

V Lombardi, G Piazzesi, M Reconditi, M Linari, L Lucii, A Stewart, Y B Sun, P Boesecke, T Narayanan, T Irving, M Irving

Research output: Contribution to journalArticlepeer-review

29 Citations (Scopus)

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 Xray 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.
Original languageEnglish
Pages (from-to)1883 - 1893
Number of pages11
JournalPhilosophical Transactions of the Royal Society of London Series B: Biological Sciences
Volume359
Issue number1452
DOIs
Publication statusPublished - 29 Dec 2004

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