title: Myosin head mechanical performance under different conformational change mechanisms.
abstract: The present paper puts forward a mathematical approach to model the conformational changes of the myosin head due to ATP hydrolysis, which determine the head swinging and consequent sliding of the actin filament. Our aim is to provide a simple but effective model simulating myosin head performance to be integrated into the overall model of sarcomere mechanics under development at our Laboratory (J. Biomech. 34 (2001) 1607). We began by exploring myosin head mechanics in recent findings about myosin ultrastructure, morphology and energetics in order to calculate the working stroke distance (WS) and the force transmitted to the actin filament during muscle contraction. Two different working stroke mechanisms were investigated, assuming that the swinging of the myosin head occurs either as a consequence of purely conformational changes (Science 261 (1993a) 58) or by thermally driven motion (ratchet mechanism) followed by conformational changes (Cell 99 (1999) 421). Our results show that force and WS values vary markedly between the two models. The maximum force generated is about 10 pN for the first model and 31 pN for the second model, and the WSs are about 13 and 4 nm, respectively. These results are then discussed and compared with published data. The experimental data used for comparison are scarce and non-homogeneous; hence, the final remarks do not lead to definite conclusions. In any event, relatively speaking, the first model is more coherent with experimental findings.
authors.affiliation: Department of Bioengineering, Politecnico di Milano, Piazza Leonardo da Vinci, 32, Milan 20133, Italy. soncini@biomed.polmi.it
authors.forename: M
authors.initials: M
authors.lastname: Soncini
authors.forename: A
authors.initials: A
authors.lastname: Redaelli
authors.forename: F M
authors.initials: FM
authors.lastname: Montevecchi
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D002645:Chickens; D008958:Models, Molecular; D009218:Myosins / Q000737:chemistry* / Q000502:physiology; D011487:Protein Conformation; D012518:Sarcomeres / Q000502:physiology
chemical_list: D009218:Myosins