scholarly journals 3-D structural analysis of the crucial intermediate of skeletal muscle myosin and its role in revised actomyosin cross-bridge cycle

BIOPHYSICS ◽  
2014 ◽  
Vol 10 (0) ◽  
pp. 89-97 ◽  
Author(s):  
Eisaku Katayama
Keyword(s):  
Skeletal Muscle ◽  
Structural Analysis ◽  
Skeletal Muscle Myosin ◽  
Cross Bridge ◽  
Muscle Myosin

Skeletal muscle myosin cross-bridge cycling is necessary for myofibrillogenesis

2003 ◽  
Vol 55 (1) ◽  
pp. 61-72 ◽  
Author(s):  
Indu Ramachandran ◽  
Monica Terry ◽  
Michael B. Ferrari
Keyword(s):  
Skeletal Muscle ◽  
Skeletal Muscle Myosin ◽  
Cross Bridge ◽  
Muscle Myosin

scholarly journals Electron microscopy of synthetic myosin filaments. Evidence for cross-bridge. Flexibility and copolymer formation.

1975 ◽  
Vol 67 (1) ◽  
pp. 93-104 ◽  
Author(s):  
T D Pollard
Keyword(s):  
Skeletal Muscle ◽  
Smooth Muscle ◽  
Structural Features ◽  
Length Frequency ◽  
Single Population ◽  
Skeletal Muscle Myosin ◽  
Distinctive Features ◽  
Myosin Filaments ◽  
The Mean ◽  
Muscle Myosin

Electron micrographs of negatively stained synthetic myosin filaments reveal that surface projections, believed to be the heads of the constituent myosin molecules, can exist in two configurations. Some filaments have the projections disposed close to the filament backbone. Other filaments have all of their projections widely spread, tethered to the backbone by slender threads. Filaments formed from the myosins of skeletal muscle, smooth muscle, and platelets each have distinctive features, particularly their lengths. Soluble mixtures of skeletal muscle myosin with either smooth muscle myosin or platelet myosin were dialyzed against 0.1 M KC1 at pH 7 to determine whether the simultaneous presence of two types of myosin would influence the properties of the filaments formed. In every case, a single population of filaments formed from the mixtures. The resulting filaments are thought to be copolymers of the two types of myosin, for several reasons: (a) their length-frequency distribution is unimodal and differs from that predicted for a simple mixture of two types of myosin filaments; (b) their mean length is intermediate between the mean lengths of the filaments formed separately from the two myosins in the mixture; (c) each of the filaments has structural features characteristic of both of the myosins in the mixture; and (d) their size and shape are determined by the proportion of the two myosins in the mixture.

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