Angle of active site of myosin heads in contracting muscle during sudden length changes View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1985-02

AUTHORS

Toshio Yanagida

ABSTRACT

The change in orientation of myosin crossbridges in contracting muscle during sudden length changes was examined by fluorescence polarization. This study used a fluorescent ATP analogue, 1,N6-etheno-2-aza-ATP(ε-2-aza-ATP) as a probe. Its fluorescence is considerably enhanced upon binding with myosin and is dependent on the chemical state of the myosin-nucleotide complex in muscle. The results showed that nucleotides bound to crossbridges in the intermediate attached state (presumably AM-ε-2-aza-ADP-Pi) during isometric contraction are highly oriented at the same angle as that of AM in rigor with bound ε-2-aza-ADP. Furthermore the orientation of nucleotides bound to crossbridges in the attached state is not altered during sudden changes in length of isometrically contracting muscle. The results of this time-resolved measurement support the conclusion obtained from a previous steady-state experiment that change in axial orientation of the active site of the myosin head is not involved in force generation. More... »

PAGES

43-52

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf00712310

DOI

http://dx.doi.org/10.1007/bf00712310

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1043902235

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/4008630


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