X-ray diffraction study of the structural changes accompanying phosphorylation of tarantula muscle.
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.
Padrón
R
R
Laboratorio de Biofísica del Músculo, Instituto Venezolano de Investigaciones Cientificas (IVIC), Caracas.
Panté
N
N
Sosa
H
H
Kendrick-Jones
J
J
D008841:Actin Cytoskeleton / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D009119:Muscle Contraction; D009132:Muscles / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure; D009218:Myosins / Q000378:metabolism; D010766:Phosphorylation; D013112:Spiders / Q000378:metabolism* / Q000502:physiology; D014961:X-Ray Diffraction
D009218:Myosins