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Myosin and Actin Filaments in Muscle: Structures and Interactions.

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Date
2017-01
ICR Author
Morris, Edward
Author
Squire, JM
Paul, DM
Morris, EP
Type
Journal Article
Metadata
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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.
URI
https://repository.icr.ac.uk/handle/internal/486
DOI
https://doi.org/10.1007/978-3-319-49674-0_11
Collections
  • Structural Biology
Subject
Sarcomeres
Animals
Humans
Myosins
Microscopy, Electron
X-Ray Diffraction
Actin Cytoskeleton
Research team
Structural Electron Microscopy
Language
eng
License start date
2017-01
Citation
Sub-cellular biochemistry, 2017, 82 pp. 319 - 371

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