A comprehensive description of the protein should include its structure,thermodynamics,and kinetic properties.The recent rise of cryogenic electron microscopy(cryo-EM)provides new opportunities for the thermodynamic and kinetic research of proteins.There have been some researches in which cryo-EM is used not only to resolve the high-resolution structure of proteins but also to analyze the conformational distribution of proteins to infer their thermodynamic properties based on data processing methods.However,whether cryo-EM can be used to directly quantify the kinetics of proteins is still unclear.In this work,an ideal protein system,cyanobacterial circadian clock protein,is selected to explore the potential of cryo-EM used to analyze the non-equilibrium process of proteins.Previous research has illustrated that cryoelectron microscope can be used to infer the thermodynamic information about the KaiC protein such as the inter-subunit interaction within the hexamers.Herein,we extend the equilibrium Ising model of KaiC hexamers to a non-equilibrium statistical physics model,revealing the properties of the non-equilibrium process of KaiC hexamers.According to the non-equilibrium model and previous biochemical research,we find that the intrinsic properties of KaiC protein allow its non-equilibrium conformational distribution to be measured by cryo-EM.
关键词
蛋白质动力学/非平衡态统计物理/冷冻电镜
Key words
protein dynamics/non-equilibrium statistical physics/cryogenic electron microscopy
维普
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