Deutsch
 
Hilfe Datenschutzhinweis Impressum
  DetailsucheBrowse

Datensatz

DATENSATZ AKTIONENEXPORT

Freigegeben

Buchkapitel

Molecular structure of the actomyosin system in cross-striated muscle

MPG-Autoren
/persons/resource/persons93463

Holmes,  Kenneth C.
Protein Cristallography XDS, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;
Muscle Research, Max Planck Institute for Medical Research, Max Planck Society;

Volltexte (beschränkter Zugriff)
Für Ihren IP-Bereich sind aktuell keine Volltexte freigegeben.
Volltexte (frei zugänglich)
Es sind keine frei zugänglichen Volltexte in PuRe verfügbar
Ergänzendes Material (frei zugänglich)
Es sind keine frei zugänglichen Ergänzenden Materialien verfügbar
Zitation

Holmes, K. C. (1972). Molecular structure of the actomyosin system in cross-striated muscle. In H. H. Weber (Ed.), Molecular Bioenergetics and Macromolecular Biochemistry (pp. 90-110). Heidelberg / Berlin: Springer.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-0019-B19D-E
Zusammenfassung
The present dogma of muscle contraction is founded principally on two tenets: (1) that contraction is the result of an interaction between actin, myosin and adenosine triphosphate (ATP), and (2) that contraction proceeds by a sliding mechanism which does not involve permanent change in the length or configuration of the component protein molecules. Actomyosin is an ATPase needing Mg++ ion as a co-factor but not Ca++ ion. The Ca++ concentration on the other hand plays a vital role in switching the muscle from a resting to an active state. I wish to acknowledge at the outset the debt we owe to Dr. H. E. Huxley for his unique role in the development of the structural ideas underlying this hypothesis.