2002
DOI: 10.1023/a:1020304420132
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Abstract: An actin filament sliding on myosin moleculesdemonstrates both longitudinal distortions and transversal fluctuationswith the linear dimension far exceeding the diameter of an actinmonomer. Local swaying of a single actin filament was identified byreading speckled fluorescent markers attached on the filament. Theaccuracy of reading each speckled marker was about 10.4 nm (r.m.s.).Longitudinal distortions of an actin filament at a low ATP concentrationof 20 μM were as much as 0.5 μm for the average filament lengt… Show more

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Cited by 4 publications
(1 citation statement)
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“…In previous works, various theoretical models have been introduced to describe motor protein motions in a gliding assay, revealing many interesting biological properties of molecular motors 29–36. However, in most cases, even though actomyosin performed 2D motion on the glass substrates, the actin movement was analyzed as if the actomyosin was performing a 1D motion along their trajectory lines, without considering the 2D nature of their motion.…”
mentioning
confidence: 99%
“…In previous works, various theoretical models have been introduced to describe motor protein motions in a gliding assay, revealing many interesting biological properties of molecular motors 29–36. However, in most cases, even though actomyosin performed 2D motion on the glass substrates, the actin movement was analyzed as if the actomyosin was performing a 1D motion along their trajectory lines, without considering the 2D nature of their motion.…”
mentioning
confidence: 99%