Abstract
The ATP synthase is a vital protein structured enzyme for energy production in our cells which synthesize the molecule adenosine tri-phosphate (ATP). ATP synthase is located at the inner membranes of mitochondria. The protein consists of two coupled rotary molecular motors, called F0 and F1, the former one being membrane embedded and the latter one being solvent exposed. Molecular motor can produce constant 40 pN·nm torque, over broad range of speed 10 to 400 rps, works in high efficiency. Structure of a rotating motor protein is very interesting and much different than classical engineering motors. Motor protein has one rotor sharing by two motors. Therefore, it rotates in two reciprocal purposes. Most of the research on ATP synthase is based on experimental observations. There are some computer simulation studies on the motor proteins to determine their mode shapes. Upon this, rotor dynamics analysis can help to estimate the correct mode shapes during the rotation and, to determine the critical rotational speeds. In this study, the dynamics of rotating motor protein will be investigated by using finite element modeling based on beam theory. Campbell diagram and resonance profiles has been obtained.
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Tirtom, I., Luo, X., Hatayama, E. (2019). Dynamic Analysis of Rotating Motor Protein (ATP Synthase) Using FEM. In: Cavalca, K., Weber, H. (eds) Proceedings of the 10th International Conference on Rotor Dynamics – IFToMM. IFToMM 2018. Mechanisms and Machine Science, vol 63. Springer, Cham. https://doi.org/10.1007/978-3-319-99272-3_25
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DOI: https://doi.org/10.1007/978-3-319-99272-3_25
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