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

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

Research output: Contribution to journalArticle

21 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)235-241
Number of pages7
JournalJournal of Muscle Research and Cell Motility
Volume12
Issue number3
DOIs
StatePublished - Jun 1991
Externally publishedYes

Fingerprint

Phosphorylation
Myosins
X-Ray Diffraction
Muscle
X ray diffraction
Muscles
Myosin Light Chains
Diffraction patterns
Electron microscopy
Electron Microscopy

ASJC Scopus subject areas

  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cell Biology

Cite this

X-ray diffraction study of the structural changes accompanying phosphorylation of tarantula muscle. / Padrón, Raúl; Panté, Nelly; Sosa, Hernando J.; Kendrick-Jones, John.

In: Journal of Muscle Research and Cell Motility, Vol. 12, No. 3, 06.1991, p. 235-241.

Research output: Contribution to journalArticle

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