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Spudich Lab
"We never met a myosin we didn't like!" |
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Spudich Lab
"We never met a myosin we didn't like!" |
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Friends and Collaborators Who's Visiting Us |
What They're Interested In |
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David says: "The molecular basis of the conversion of the chemical energy of ATP hydrolysis into mechanical movement by myosin has reached a detailed level of analysis, thanks to in vitro assays for measuring myosin movement along actin filaments. Using these assays, myosin V has been shown to move in 36-nm steps along its actin track. Two distinct sub-steps of the overall 36-nm step of myosin V, a working stroke of 25 nm followed by a diffusional step of 11 nm have also been discovered. "In vitro motility assays, single molecule experiments, cryo EM, and crystal structures have helped to understand the mechanism of force production by myosin V. However, none of these techniques provide a complete description of all the steps involved in myosin V processivity. The goal of my research is to create a computational model integrating biophysical, structural, and experimental date that will simulate the processivity of myosin V." |
 Research Associate, Delp Lab Dept. of Bioengineering Stanford University liaojc@stanford.edu |
Jung-Chi says:
"Myosins convert ATP chemical energy into mechanical work such as muscle contractions or actin-based transports. It is important to link the structural information and the experimental data together by suitable computational models to understand this mechanochemical energy transduction. Both kinetic models and mechanochemical models (advection-reaction-diffusion equations) are used to study these motor proteins. Specifically, I construct models for myosin V first and extend the developed tools to study other myosin classes such myosin VI and myosin II. The final goal is to build structure-based coarse-grained models consistent with experimental measurements." |
 Zev Bryant
Assistant Professor Dept. of Bioengineering Stanford University zevry@stanford.edu |
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Graduate Student, Bryant Lab Dept. of Bioengineering Stanford University mrn@stanford.edu |
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