A physical model for motor proteins.
A general stochastic theory is outlined for chemical to mechanical energy transduction by motor enzymes. In addition to ATP hydrolysis and fiber binding phenomena, thermal noise effects are taken into account. A minimal, 4-state model is identified that gives the hydrolysis rate as well as mechanical quantities such as sliding velocity and generated force, as functions of ATP concentration and the number of motors. It explains in a unified way many results of recent in vitro assays, both in myosins/actin and kinesins or dyneins/microtubule systems.
Leibler
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Service de Physique théorique, Centre d'Etudes de Saclay, Gif-sur-Yvette.
Huse
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DA
D008956:Models, Chemical; D008962:Models, Theoretical; D009124:Muscle Proteins / Q000737:chemistry*; D055585:Physical Phenomena; D010825:Physics; D013269:Stochastic Processes
D009124:Muscle Proteins