ArticleThe Journal of chemical physics2018
Efficient use of single molecule time traces to resolve kinetic rates, models and uncertainties.
Article in The Journal of chemical physics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- 14-3-3τ as a Modulator of Early α-Synuclein Multimerization and Amyloid Formation.ACS chemical neuroscience · 2024Article
- Heterogeneous migration routes of DNA triplet repeat slip-outs.Biophysical reports · 2022Article
- Can DyeCycling break the photobleaching limit in single-molecule FRET?Nano research · 2022Article
- KERA: analysis tool for multi-process, multi-state single-molecule data.Nucleic acids research · 2021Article
- Illuminating amyloid fibrils: Fluorescence-based single-molecule approaches.Computational and structural biotechnology journal · 2021Review
- Article
- Metal ions and sugar puckering balance single-molecule kinetic heterogeneity in RNA and DNA tertiary contacts.Nature communications · 2020Article
- Conformational Cycling within the Closed State of Grp94, an Hsp90-Family Chaperone.Journal of molecular biology · 2019Article
- Precision and accuracy of single-molecule FRET measurements-a multi-laboratory benchmark study.Nature methods · 2018Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Single molecule time traces reveal the time evolution of unsynchronized kinetic systems. Especially single molecule Förster resonance energy transfer (smFRET) provides access to enzymatically important time scales, combined with molecular distance resolution and minimal interference with the sample. Yet the kinetic analysis of smFRET time traces is complicated by experimental shortcomings-such as photo-bleaching and noise. Here we recapitulate the fundamental limits of single molecule fluorescence that render the classic, dwell-time based kinetic analysis unsuitable. In contrast, our Single Molecule Analysis of Complex Kinetic Sequences (SMACKS) considers every data point and combines the information of many short traces in one global kinetic rate model. We demonstrate the potential of SMACKS by resolving the small kinetic effects caused by different ionic strengths in the chaperone protein Hsp90. These results show an unexpected interrelation between conformational dynamics and ATPase activity in Hsp90.
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Registered trials
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