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 |
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Pages (from-to) | 181-189 |
Number of pages | 9 |
Journal | Nature Nanotechnology |
Volume | 16 |
Issue number | 2 |
DOIs | |
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