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Mechanics of myosin function in white muscle fibres of the dogfish, Scyliorhinus canicula
Author(s) -
ParkHolohan S.,
Linari M.,
Reconditi M.,
Fusi L.,
Brunello E.,
Irving M.,
Dolfi M.,
Lombardi V.,
West T. G.,
Curtin N. A.,
Woledge R. C.,
Piazzesi G.
Publication year - 2012
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2011.217133
Subject(s) - scyliorhinus canicula , myosin , white (mutation) , anatomy , biology , chemistry , biophysics , fish <actinopterygii> , fishery , genetics , gene
Key points • Muscle force and shortening are generated by a structural change called the working stroke in myosin motor proteins that cross‐link the myosin and actin filaments in muscle. • Precise values for two key parameters of the myosin motor – its mechanical stiffness and the size of the working stroke at low load – were previously only available from one type of muscle in one species, fast twitch muscles of the frog, so it was not clear how generally applicable these values were. • We show that in dogfish fast muscle the low‐load working stroke is the same as in frog muscle, but the myosin motor stiffness is smaller. • The results provide new insights into how the molecular properties of myosin motors in different muscle types and species may be adapted for different muscle functions.