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^*

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

79 Scopus citations

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.

Original language	English
Pages (from-to)	181-189
Number of pages	9
Journal	Nature Nanotechnology
Volume	16
Issue number	2
DOIs	https://doi.org/10.1038/s41565-020-00798-9
State	Published - 2021/02

ASJC Scopus subject areas

Bioengineering
Atomic and Molecular Physics, and Optics
Biomedical Engineering
General Materials Science
Condensed Matter Physics
Electrical and Electronic Engineering

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10.1038/s41565-020-00798-9

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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

@article{843ad05c0c8741a298ab5b3e0f5a532e,

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",

note = "Publisher Copyright: {\textcopyright} 2020, The Author(s), under exclusive licence to Springer Nature Limited.",

year = "2021",

month = feb,

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

language = "英語",

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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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T1 - Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy

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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SP - 181

EP - 189

JO - Nature Nanotechnology

JF - Nature Nanotechnology

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ER -

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

Abstract

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