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. 1991 Jun;12(3):235-41.
doi: 10.1007/BF01745112.

X-ray Diffraction Study of the Structural Changes Accompanying Phosphorylation of Tarantula Muscle

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X-ray Diffraction Study of the Structural Changes Accompanying Phosphorylation of Tarantula Muscle

R Padrón et al. J Muscle Res Cell Motil. .

Abstract

Electron microscopy of negatively stained isolated thick filaments of tarantula muscle has revealed that phosphorylation of myosin regulatory light chains is accompanied by a loss of the helical order of myosin heads. From equatorial X-ray diffraction patterns of tarantula muscles in the phosphorylated state we have detected a mass movement in the myosin filaments that supports this finding.

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