Article ; Online: Single-molecule FRET for virology: 20 years of insight into protein structure and dynamics.
Quarterly reviews of biophysics
2023 Volume 56, Page(s) e3
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 ... ...
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. |
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MeSH term(s) | Fluorescence Resonance Energy Transfer/methods ; Cryoelectron Microscopy ; Protein Conformation ; Nucleic Acids ; Viral Proteins |
Chemical Substances | Nucleic Acids ; Viral Proteins |
Language | English |
Publishing date | 2023-05-18 |
Publishing country | England |
Document type | Journal Article ; Review ; Research Support, Non-U.S. Gov't |
ZDB-ID | 209912-3 |
ISSN | 1469-8994 ; 0033-5835 |
ISSN (online) | 1469-8994 |
ISSN | 0033-5835 |
DOI | 10.1017/S0033583523000021 |
Database | MEDical Literature Analysis and Retrieval System OnLINE |
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