AI Article Synopsis
- Intrinsically disordered proteins (IDPs) are proteins that lack a fixed shape, playing crucial roles in various biological processes due to their ability to adopt multiple structures.
- The dynamic nature of IDPs makes it challenging to analyze their structures, but high-speed atomic force microscopy (HS-AFM) offers a promising method for studying these proteins.
- Using HS-AFM, researchers can capture images that reveal the different conformations of IDPs, identify regions that are consistently folded or disordered, and estimate the number of amino acids in disordered segments, providing insight into their dynamic behavior.
Article 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.
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| http://dx.doi.org/10.1038/s41565-020-00798-9 | DOI Listing |
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