FRET-Mediated Observation of Protein-Triggered Conformational Changes in DNA Nanostructures

Single-Nucleobase-Resolved Nanoruler Determines the Surface Energy Transfer Radius on the Living Cell Membrane

“…Distance-dependent energy transfer between a pair of a donor and an acceptor could be the most effective and practical optical nanoruler for sensing, imaging, and tracking biological and chemical events, such as protein–protein interactions, in vitro or in vivo imaging, protein conformational changes, , nucleic acid analysis, − binding site identification, , molecular tension measurements, etc . For example, Förster resonant energy transfer (FRET) proposed by Förster in 1948 opens up a new avenue for optical imaging − and tracking conformational changes of biological molecules, − as well as understanding deeper biochemical processes. − In FRET, two fluorophore molecular dipoles act as the donor and acceptor, which has a limited distance scale of less than 10 nm and greatly limits the detection of a broader range of molecular events.…”