Evidence map›Paper›PMID 19630372›Full record

ArticleThe journal of physical chemistry. B2009

Extracting kinetics information from single-molecule fluorescence resonance energy transfer data using hidden markov models.

Tae-Hee Lee

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

38 citing papers in PubMed.

  1. Single-molecule dissection of CFTR folding defects and pharmacological rescue.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  12. Theory and Analysis of Single-Molecule FRET Experiments.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  13. Article
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  15. Review
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  18. Physical Chemistry of Epigenetics: Single-Molecule Investigations.The journal of physical chemistry. B · 2019
    Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

1 author.

Tae-Hee LeeDepartment of Chemistry, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

Funding

Dynamics in Translation: the Role of Fluctuation in Protein SynthesisR00GM079960 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI LEE, TAE-HEE · 2007 to 2009
$729k
Dynamics in Translation: the Role of Fluctuation in Protein SynthesisK99GM079960 · NIGMS · STANFORD UNIVERSITY · PI LEE, TAE-HEE · 2007 to 2007
$59k
NIGMS NIH HHS GM079960NIGMS NIH HHS K99 GM079960NIGMS NIH HHS R00 GM079960
6 · The paper itself

Abstract

Hidden Markov models (HMM) have been proposed as a method of analysis for noisy single-molecule fluorescence resonance energy transfer (SM FRET) data. However, there are practical and fundamental limits in applying HMM to SM FRET data due to the short photobleaching lifetimes of fluorophores and the limited time resolution of detection devices. The fast photobleaching fluorophores yield short SM FRET time traces, and the limited detection time resolution generates abnormal FRET values, which result in systematic underestimation of kinetic rates. In this work, a HMM algorithm is implemented to optimize one set of HMM parameters with multiple short SM FRET traces. The FRET efficiency distribution function for the HMM optimization was modified to accommodate the abnormal FRET values resulting from limited detection time resolution. Computer simulations reveal that one set of HMM parameters is optimized successfully using multiple short SM FRET traces and that the degree of the kinetic rate underestimation is reduced by using the proposed modified FRET efficiency distribution. In conclusion, it is demonstrated that HMM can be used to reproducibly analyze short SM FRET time traces.

Indexed as

Fluorescence Resonance Energy TransferMarkov ChainsAlgorithmsKinetics

Identifiers

PMID19630372
PMCPMC8785102

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.