The conformation of myosin head domains in rigor muscle determined by X-ray interference

M Reconditi, N Koubassova, M Linari, I Dobbie, T Narayanan, O Diat, G Piazzesi, V Lombardi, M Irving

Research output: Contribution to journalArticlepeer-review

30 Citations (Scopus)

Abstract

In the absence of adenosine triphosphate, the head domains of myosin cross-bridges in muscle bind to actin filaments in a rigor conformation that is expected to mimic that following the working stroke during active contraction. We used x-ray interference between the two head arrays in opposite halves of each myosin filament to determine the rigor head conformation in single fibers from frog skeletal muscle. During isometric contraction (force T-0), the interference effect splits the M3 x-ray reflection from the axial repeat of the heads into two peaks with relative intensity (higher angle/lower angle peak) 0.76. In demembranated fibers in rigor at low force (
Original languageEnglish
Pages (from-to)1098 - 1110
Number of pages13
JournalBiophysical Journal
Volume85
Issue number2
DOIs
Publication statusPublished - 1 Aug 2003

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