Myosin and Actin Filaments in Muscle: Structures and Interactions.
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ICR Authors
Authors
Squire, JM
Paul, DM
Morris, EP
Paul, DM
Morris, EP
Document Type
Journal Article
Date
2017-01-01
Date Accepted
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.
Citation
Sub-cellular biochemistry, 2017, 82 pp. 319 - 371
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Source Title
Publisher
SPRINGER INTERNATIONAL PUBLISHING AG
ISSN
0306-0225
eISSN
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Research Team
Structural Electron Microscopy