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Subcell Biochem. 2017;82:319-371. doi: 10.1007/978-3-319-49674-0_11.

Myosin and Actin Filaments in Muscle: Structures and Interactions.

Author information

1
Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK. j.squire@imperial.ac.uk.
2
Muscle Contraction Group, School of Physiology, Pharmacology and Neuroscience, University of Bristol, Bristol, BS8 1TD, UK.
3
Division of Structural Biology, The Institute of Cancer Research, London, SW3 6JB, UK.

Abstract

In the last decade, improvements in electron microscopy and image processing have permitted significantly higher resolutions to be achieved (sometimes <1 nm) when studying isolated actin and myosin filaments. In the case of actin filaments the changing structure when troponin binds calcium ions can be followed using electron microscopy and single particle analysis to reveal what happens on each of the seven non-equivalent pseudo-repeats of the tropomyosin α-helical coiled-coil. In the case of the known family of myosin filaments not only are the myosin head arrangements under relaxing conditions being defined, but the latest analysis, also using single particle methods, is starting to reveal the way that the α-helical coiled-coil myosin rods are packed to give the filament backbones.

KEYWORDS:

C-protein; Muscle thick filaments; Myosin binding protein-C; Myosin rod packing; Nebulin; Paramyosin; Titin; Tropomyosin; Troponin

PMID:
28101867
DOI:
10.1007/978-3-319-49674-0_11
[Indexed for MEDLINE]

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