Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy

Noriyuki Kodera; Daisuke Noshiro; Sujit K. Dora; Tetsuya Mori; Johnny Habchi; David Blocquel; Antoine Gruet; Marion Dosnon; Edoardo Salladini; Christophe Bignon; Yuko Fujioka; Takashi Oda; Nobuo N. Noda; Mamoru Sato; Marina Lotti; Mineyuki Mizuguchi; Sonia Longhi; Toshio Ando

doi:10.1038/s41565-020-00798-9

Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy

Noriyuki Kodera, Daisuke Noshiro, Sujit K. Dora, Tetsuya Mori, Johnny Habchi, David Blocquel, Antoine Gruet, Marion Dosnon, Edoardo Salladini, Christophe Bignon, Yuko Fujioka, Takashi Oda, Nobuo N. Noda, Mamoru Sato, Marina Lotti, Mineyuki Mizuguchi, Sonia Longhi^*, Toshio Ando^*

^*この論文の責任著者

構造生物学研究室

研究成果: ジャーナルへの寄稿 › 学術論文 › 査読

79 被引用数 (Scopus)

抄録

Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude of conformational states, thus rendering their structural analysis very difficult. Here we explore the potential of high-speed atomic force microscopy (HS-AFM) for characterizing the structure and dynamics of IDPs. Successive HS-AFM images of an IDP molecule can not only identify constantly folded and constantly disordered regions in the molecule, but can also document disorder-to-order transitions. Moreover, the number of amino acids contained in these disordered regions can be roughly estimated, enabling a semiquantitative, realistic description of the dynamic structure of IDPs.

本文言語	英語
ページ（範囲）	181-189
ページ数	9
ジャーナル	Nature Nanotechnology
巻	16
号	2
DOI	https://doi.org/10.1038/s41565-020-00798-9
出版ステータス	出版済み - 2021/02

ASJC Scopus 主題領域

バイオエンジニアリング
原子分子物理学および光学
生体医工学
材料科学一般
凝縮系物理学
電子工学および電気工学

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10.1038/s41565-020-00798-9

引用スタイル

Kodera, N., Noshiro, D., Dora, S. K., Mori, T., Habchi, J., Blocquel, D., Gruet, A., Dosnon, M., Salladini, E., Bignon, C., Fujioka, Y., Oda, T., Noda, N. N., Sato, M., Lotti, M., Mizuguchi, M., Longhi, S., & Ando, T. (2021). Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. Nature Nanotechnology, 16(2), 181-189. https://doi.org/10.1038/s41565-020-00798-9

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title = "Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy",

abstract = "Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude of conformational states, thus rendering their structural analysis very difficult. Here we explore the potential of high-speed atomic force microscopy (HS-AFM) for characterizing the structure and dynamics of IDPs. Successive HS-AFM images of an IDP molecule can not only identify constantly folded and constantly disordered regions in the molecule, but can also document disorder-to-order transitions. Moreover, the number of amino acids contained in these disordered regions can be roughly estimated, enabling a semiquantitative, realistic description of the dynamic structure of IDPs.",

author = "Noriyuki Kodera and Daisuke Noshiro and Dora, {Sujit K.} and Tetsuya Mori and Johnny Habchi and David Blocquel and Antoine Gruet and Marion Dosnon and Edoardo Salladini and Christophe Bignon and Yuko Fujioka and Takashi Oda and Noda, {Nobuo N.} and Mamoru Sato and Marina Lotti and Mineyuki Mizuguchi and Sonia Longhi and Toshio Ando",

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doi = "10.1038/s41565-020-00798-9",

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Kodera, N, Noshiro, D, Dora, SK, Mori, T, Habchi, J, Blocquel, D, Gruet, A, Dosnon, M, Salladini, E, Bignon, C, Fujioka, Y, Oda, T, Noda, NN, Sato, M, Lotti, M, Mizuguchi, M, Longhi, S & Ando, T 2021, 'Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy', Nature Nanotechnology, vol. 16, no. 2, pp. 181-189. https://doi.org/10.1038/s41565-020-00798-9

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AU - Kodera, Noriyuki

AU - Noshiro, Daisuke

AU - Dora, Sujit K.

AU - Mori, Tetsuya

AU - Habchi, Johnny

AU - Blocquel, David

AU - Gruet, Antoine

AU - Dosnon, Marion

AU - Salladini, Edoardo

AU - Bignon, Christophe

AU - Fujioka, Yuko

AU - Oda, Takashi

AU - Noda, Nobuo N.

AU - Sato, Mamoru

AU - Lotti, Marina

AU - Mizuguchi, Mineyuki

AU - Longhi, Sonia

AU - Ando, Toshio

PY - 2021/2

Y1 - 2021/2

N2 - Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude of conformational states, thus rendering their structural analysis very difficult. Here we explore the potential of high-speed atomic force microscopy (HS-AFM) for characterizing the structure and dynamics of IDPs. Successive HS-AFM images of an IDP molecule can not only identify constantly folded and constantly disordered regions in the molecule, but can also document disorder-to-order transitions. Moreover, the number of amino acids contained in these disordered regions can be roughly estimated, enabling a semiquantitative, realistic description of the dynamic structure of IDPs.

AB - Intrinsically disordered proteins (IDPs) are ubiquitous proteins that are disordered entirely or partly and play important roles in diverse biological phenomena. Their structure dynamically samples a multitude of conformational states, thus rendering their structural analysis very difficult. Here we explore the potential of high-speed atomic force microscopy (HS-AFM) for characterizing the structure and dynamics of IDPs. Successive HS-AFM images of an IDP molecule can not only identify constantly folded and constantly disordered regions in the molecule, but can also document disorder-to-order transitions. Moreover, the number of amino acids contained in these disordered regions can be roughly estimated, enabling a semiquantitative, realistic description of the dynamic structure of IDPs.

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Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy

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