AI Article Synopsis
- Classical structural biology offers only static images of biomacromolecules, while single-molecule Förster resonance energy transfer (smFRET) allows researchers to study the dynamic behavior of these structures in realistic biological conditions.
- Since its introduction in 1996, smFRET has validated existing theories and unveiled new information about essential biological processes, including DNA repair, transcription, translation, and membrane transport.
- The review examines two decades of smFRET's contributions to biochemistry and proposes future applications like biosensing, high-throughput screening, and molecular diagnostics, building on advanced smFRET techniques.
Article Abstract
Classical structural biology can only provide static snapshots of biomacromolecules. Single-molecule Förster resonance energy transfer (smFRET) paved the way for studying dynamics in macromolecular structures under biologically relevant conditions. Since its first implementation in 1996, smFRET experiments have confirmed previously hypothesized mechanisms and provided new insights into many fundamental biological processes, such as DNA maintenance and repair, transcription, translation, and membrane transport. We review 22 years of contributions of smFRET to our understanding of basic mechanisms in biochemistry, molecular biology, and structural biology. Additionally, building on current state-of-the-art implementations of smFRET, we highlight possible future directions for smFRET in applications such as biosensing, high-throughput screening, and molecular diagnostics.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6200918 | PMC |
| http://dx.doi.org/10.1126/science.aan1133 | DOI Listing |
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