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- W4311399587 endingPage "1876" @default.
- W4311399587 startingPage "1876" @default.
- W4311399587 abstract "The unique functions of intrinsically disordered proteins (IDPs) depend on their dynamic protean structure that often eludes analysis. High-speed atomic force microscopy (HS-AFM) can conduct this difficult analysis by directly visualizing individual IDP molecules in dynamic motion at sub-molecular resolution. After brief descriptions of the microscopy technique, this review first shows that the intermittent tip–sample contact does not alter the dynamic structure of IDPs and then describes how the number of amino acids contained in a fully disordered region can be estimated from its HS-AFM images. Next, the functional relevance of a dumbbell-like structure that has often been observed on IDPs is discussed. Finally, the dynamic structural information of two measles virus IDPs acquired from their HS-AFM and NMR analyses is described together with its functional implications." @default.
- W4311399587 created "2022-12-26" @default.
- W4311399587 creator A5056997297 @default.
- W4311399587 date "2022-12-14" @default.
- W4311399587 modified "2023-09-25" @default.
- W4311399587 title "Functional Implications of Dynamic Structures of Intrinsically Disordered Proteins Revealed by High-Speed AFM Imaging" @default.
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