@article{oai:kanazawa-u.repo.nii.ac.jp:00040002,
 author = {淺川, 雅 and 福間, 剛士 and Asakawa, Hitoshi and Ikegami, Koji and Setou, Mitsutoshi and Watanabe, Naoki and Tsukada, Masaru and Fukuma, Takeshi},
 issue = {5},
 journal = {Biophysical Journal},
 month = {Sep},
 note = {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. © 2011 Biophysical Society., 金沢大学ナノマテリアル研究所},
 pages = {1270--1276},
 title = {Submolecular-scale imaging of α-helices and C-terminal domains of tubulins by frequency modulation atomic force microscopy in liquid},
 volume = {101},
 year = {2011}
}