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- W2079084402 abstract "In this study, we directly imaged subnanometer-scale structures of tubulins by performing frequency modulation atomic force microscopy (FM-AFM) in liquid. Individual α-helices at the surface of a tubulin protofilament were imaged as periodic corrugations with a spacing of 0.53 nm, which corresponds to the common pitch of an α-helix backbone (0.54 nm). The identification of individual α-helices allowed us to determine the orientation of the deposited tubulin protofilament. As a result, C-terminal domains of tubulins were identified as protrusions with a height of 0.4 nm from the surface of the tubulin. The imaging mechanism for the observed subnanometer-scale contrasts is discussed in relation to the possible structures of the C-terminal domains. Because the C-terminal domains are chemically modified to regulate the interactions between tubulins and other biomolecules (e.g., motor proteins and microtubule-associated proteins), detailed structural information on individual C-terminal domains is valuable for understanding such regulation mechanisms. The results obtained in this study demonstrate that FM-AFM is capable of visualizing the structural variation of tubulins with subnanometer resolution. This is an important first step toward using FM-AFM to analyze the functions of tubulins." @default.
- W2079084402 created "2016-06-24" @default.
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- W2079084402 date "2011-09-01" @default.
- W2079084402 modified "2023-10-06" @default.
- W2079084402 title "Submolecular-Scale Imaging of α-Helices and C-Terminal Domains of Tubulins by Frequency Modulation Atomic Force Microscopy in Liquid" @default.
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- W2079084402 doi "https://doi.org/10.1016/j.bpj.2011.07.020" @default.
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