X-ray diffraction study of the structural changes accompanying phosphorylation of tarantula muscle

Raúl Padrón, Nelly Panté, Hernando Sosa, John Kendrick-Jones

Research output: Contribution to journalArticle

21 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)235-241
Number of pages7
JournalJournal of Muscle Research and Cell Motility
Issue number3
Publication statusPublished - Jun 1 1991
Externally publishedYes


ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Cell Biology

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