Myosin and actin filaments in muscle: structures and interactions

JM Squire, DM Paul, EP Morris - Fibrous proteins: Structures and …, 2017 - Springer
Fibrous proteins: Structures and mechanisms, 2017Springer
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 …
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.
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