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Title: Minimum structural unit required for energy transduction in muscle. Author: Yanagida T, Harada Y. Journal: Adv Exp Med Biol; 1988; 226():277-87. PubMed ID: 3407516. Abstract: The sliding of actin filaments was directly measured along single-headed myosin filaments on which the density of the heads was widely varied, using video-fluorescence microscopy. The results showed that the double-headed structure of myosin is not essential for inducing the sliding movement of actin filaments. The minimum number of myosin heads required for supporting movement of actin filaments at a maximum velocity of 5 micron/s at 23 degrees C was estimated to be 4, at most 16. This led to the conclusion that the sliding distance of actin filaments induced during a single ATP hydrolysis cycle is probably 160 nm or more, at least 40 nm under unloaded conditions.[Abstract] [Full Text] [Related] [New Search]