Abstract
Intrinsically disordered proteins (IDPs) are highly abundant in nature and play vital roles in various biological processes. Understanding their biological functions requires extracting their exact conformations, which remains a technical challenge, especially in living cells, due to the exceptional spatiotemporal heterogeneity of IDPs. Here we develop an experimental approach using site-specific fluorescent labeling of IDPs in non-fixed cells and fluorescent lifetime imaging microscopy (FLIM) to directly decipher their plasticity via FRET.
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