title: X-ray diffraction study of the structural changes accompanying phosphorylation of tarantula muscle.
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.
authors.affiliation: Laboratorio de Biofísica del Músculo, Instituto Venezolano de Investigaciones Cientificas (IVIC), Caracas.
authors.forename: R
authors.initials: R
authors.lastname: Padrón
authors.forename: N
authors.initials: N
authors.lastname: Panté
authors.forename: H
authors.initials: H
authors.lastname: Sosa
authors.forename: J
authors.initials: J
authors.lastname: Kendrick-Jones
mesh_terms: 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
chemical_list: D009218:Myosins