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.

Kodera, N., Noshiro, D., Dora, S., Mori, T., Habchi, J., Blocquel, D., et al. (2021). Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. NATURE NANOTECHNOLOGY, 16(2), 181-189 [10.1038/s41565-020-00798-9].

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

Lotti M.;
2021

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.
Articolo in rivista - Articolo scientifico
Intrinsically disordered proteins, conformation, disorder to order transition, high speed atomic force microscopy
English
23-nov-2020
2021
16
2
181
189
reserved
Kodera, N., Noshiro, D., Dora, S., Mori, T., Habchi, J., Blocquel, D., et al. (2021). Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy. NATURE NANOTECHNOLOGY, 16(2), 181-189 [10.1038/s41565-020-00798-9].
File in questo prodotto:
File Dimensione Formato  
Kodera-2021-Nature Nanotechnol-VoR.pdf

Solo gestori archivio

Tipologia di allegato: Publisher’s Version (Version of Record, VoR)
Licenza: Tutti i diritti riservati
Dimensione 7.2 MB
Formato Adobe PDF
7.2 MB Adobe PDF   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/295727
Citazioni
  • Scopus 68
  • ???jsp.display-item.citation.isi??? 54
Social impact