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

Autor: Edoardo Salladini, Yuko Fujioka, Marina Lotti, David Blocquel, Antoine Gruet, Noriyuki Kodera, Daisuke Noshiro, Nobuo N. Noda, Mineyuki Mizuguchi, Tetsuya Mori, Mamoru Sato, Marion Dosnon, Christophe Bignon, Takashi Oda, Sonia Longhi, Johnny Habchi, Sujit Kumar Dora, Toshio Ando
Přispěvatelé: Kodera, N, Noshiro, D, Dora, S, Mori, T, Habchi, J, Blocquel, D, Gruet, A, Dosnon, M, Salladini, E, Bignon, C, Fujioka, Y, Oda, T, Noda, N, Sato, M, Lotti, M, Mizuguchi, M, Longhi, S, Ando, T, Architecture et fonction des macromolécules biologiques (AFMB), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Institut National de Recherche pour l’Agriculture, l’Alimentation et l’Environnement (INRAE), Aix Marseille Université (AMU), Kanazawa University (KU), Academy of Performing Arts [Prague] (AMU), The Institute of Statistical Mathematics (Tokyo ), Yokohama National University, Università degli Studi di Milano-Bicocca [Milano] (UNIMIB), University of Toyama
Jazyk: angličtina
Rok vydání: 2021
Předmět:
Protein Folding
Materials science
Protein Conformation
Biomedical Engineering
Quantitative Structure-Activity Relationship
Bioengineering
02 engineering and technology
010402 general chemistry
Intrinsically disordered proteins
Microscopy
Atomic Force
01 natural sciences
Protein structure
Microscopy
Molecule
Humans
General Materials Science
[SDV.BBM]Life Sciences [q-bio]/Biochemistry
Molecular Biology
Electrical and Electronic Engineering
Intrinsically disordered proteins
conformation
disorder to order transition
high speed atomic force microscopy
ComputingMilieux_MISCELLANEOUS
Atomic force microscopy
Dynamics (mechanics)
021001 nanoscience & nanotechnology
Condensed Matter Physics
Atomic and Molecular Physics
and Optics
0104 chemical sciences
Molecular Imaging
Intrinsically Disordered Proteins
Chemical physics
Mutation
Protein folding
0210 nano-technology
Zdroj: Nature Nanotechnology
Nature Nanotechnology, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
Nature Nanotechnology, Nature Publishing Group, 2021, 16 (2), pp.181-189. ⟨10.1038/s41565-020-00798-9⟩
ISSN: 1748-3387
1748-3395
Popis: International audience; High-speed AFM imaging enables a semiquantitative, realistic description of the dynamic structure of intrinsically disordered proteins.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.
Databáze: OpenAIRE
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