Simultaneous Measurement of Individual ATPase and Mechanical Reactions by a Single Myosin Molecule at Work View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1999-01

AUTHORS

Akihiko Ishijima, Hiroaki Kojima, Hiroto Tanaka, Toshio Yanagida

ABSTRACT

Based on techniques for single molecule imaging and nanomanipulation by optical tweezers, we have developed a new technique that allows simultaneous measurement of individual ATPase and mechanical reactions from a single myosin molecule during force generation. We show how the ATPase reaction couples to the mechanical reaction directly at the single molecule level. The results show that the myosin head can produce force even after releasing the bound nucleotide, probably ADP, suggesting that the chemical energy driven by ATP hydrolysis can be hysteretically stored in the myosin molecule. This view does not support a widely accepted hypothesis in which the force generation is tightly coupled to ligand dissociation. More... »

PAGES

16-23

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10043-999-0016-5

DOI

http://dx.doi.org/10.1007/s10043-999-0016-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1040037411


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