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- W4377011757 abstract "Abstract Although viral protein structure and replication mechanisms have been explored extensively with X-ray crystallography, cryo-electron microscopy, and population imaging studies, these methods are often not able to distinguish dynamic conformational changes in real time. Single-molecule fluorescence resonance energy transfer (smFRET) offers unique insights into interactions and states that may be missed in ensemble studies, such as nucleic acid or protein structure, and conformational transitions during folding, receptor–ligand interactions, and fusion. We discuss the application of smFRET to the study of viral protein conformational dynamics, with a particular focus on viral glycoprotein dynamics, viral helicases, proteins involved in HIV reverse transcription, and the influenza RNA polymerase. smFRET experiments have played a crucial role in deciphering conformational changes in these processes, emphasising the importance of smFRET as a tool to help elucidate the life cycle of viral pathogens and identify key anti-viral targets." @default.
- W4377011757 created "2023-05-19" @default.
- W4377011757 creator A5024083957 @default.
- W4377011757 creator A5036459067 @default.
- W4377011757 creator A5042649027 @default.
- W4377011757 creator A5058445771 @default.
- W4377011757 date "2023-01-01" @default.
- W4377011757 modified "2023-10-18" @default.
- W4377011757 title "Single-molecule FRET for virology: 20 years of insight into protein structure and dynamics" @default.
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