Evidence map›Paper›PMID 17344321›Full record

ArticleNucleic acids research2007

Mg2+-dependent folding of a Diels-Alderase ribozyme probed by single-molecule FRET analysis.

Andrei Yu Kobitski, Alexander Nierth, Mark Helm, Andres Jäschke, G Ulrich Nienhaus

Abstract read
In one paragraph

Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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

23 citing papers in PubMed.

  1. Cooperativity and Allostery in RNA Systems.Methods in molecular biology (Clifton, N.J.) · 2021
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  16. DNA as a versatile chemical component for catalysis, encoding, and stereocontrol.Angewandte Chemie (International ed. in English) · 2010
    Review
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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

5 authors.

Andrei Yu KobitskiInstitute of Biophysics, University of Ulm, 89069 Ulm, Germany.
Alexander Nierth
Mark Helm
Andres Jäschke
G Ulrich Nienhaus

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we report a single-molecule fluorescence resonance energy transfer (FRET) study of a Diels-Alderase (DAse) ribozyme, a 49-mer RNA with true catalytic properties. The DAse ribozyme was labeled with Cy3 and Cy5 as a FRET pair of dyes to observe intramolecular folding, which is a prerequisite for its recognition and turnover of two organic substrate molecules. FRET efficiency histograms and kinetic data were taken on a large number of surface-immobilized ribozyme molecules as a function of the Mg(2+) concentration in the buffer solution. From these data, three separate states of the DAse ribozyme can be distinguished, the unfolded (U), intermediate (I) and folded (F) states. A thermodynamic model was developed to quantitatively analyze the dependence of these states on the Mg(2+) concentration. The FRET data also provide information on structural properties. The I state shows a strongly cooperative compaction with increasing Mg(2+) concentration that arises from association with several Mg(2+) ions. This transition is followed by a second Mg(2+)-dependent cooperative transition to the F state. The observation of conformational heterogeneity and continuous fluctuations between the I and F states on the approximately 100 ms timescale offers insight into the folding dynamics of this ribozyme.

Indexed as

Cations, DivalentFluorescence Resonance Energy TransferMagnesiumModels, MolecularNucleic Acid ConformationRNA, CatalyticThermodynamicsCations, DivalentMagnesiumRNA, Catalytic

Identifiers

PMID17344321
PMCPMC1874616

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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.