Nature nanotechnology, 2021-02, Vol.16 (2), p.181-189
2021
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Details
- Autor(en) / Beteiligte
- Titel
- Structural and dynamics analysis of intrinsically disordered proteins by high-speed atomic force microscopy
- Ist Teil von
- Nature nanotechnology, 2021-02, Vol.16 (2), p.181-189
- Ort / Verlag
- England: Nature Publishing Group
- Erscheinungsjahr
- 2021
- Quelle
- Nature_系列刊
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1748-3387eISSN: 1748-3395DOI: 10.1038/s41565-020-00798-9Titel-ID: cdi_hal_primary_oai_HAL_hal_03362314v1
- Format
- –
- Schlagworte
- Amino acids, Atomic force microscopy, Biochemistry, Molecular Biology, Dynamic structural analysis, High speed, Humans, Intrinsically Disordered Proteins - chemistry, Intrinsically Disordered Proteins - genetics, Intrinsically Disordered Proteins - metabolism, Life Sciences, Microscopes, Microscopy, Microscopy, Atomic Force, Molecular Imaging, Mutation, Protein Conformation, Protein Folding, Proteins, Quantitative Structure-Activity Relationship, Structural analysis