Evidence map›Paper›PMID 15695587›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Stretched exponential decay and correlations in the catalytic activity of fluctuating single lipase molecules.

Ophir Flomenbom, Kelly Velonia, Davey Loos, Sadahiro Masuo, Mircea Cotlet, Yves Engelborghs, Johan Hofkens, Alan E Rowan, Roeland J M Nolte, Mark Van der Auweraer and 2 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
12.2field-weighted citation impact, top 1% of its field
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

55 citing papers in PubMed, 293 citations in OpenAlex.

  1. Article
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  4. Memory effects of transcription regulator-DNA interactions in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  12. Effect of the PHY Domain on the Photoisomerization Step of the Forward PChemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  13. The interplay between chromophore and protein determines the extended excited state dynamics in a single-domain phytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2020
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  14. Article
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  19. Slow domain reconfiguration causes power-law kinetics in a two-state enzyme.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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

12 authors at 2 institutions in 2 countries.

Ophir FlomenbomSchool of Chemistry, Raymond and Beverly Sackler Faculty of Exact Sciences, Tel Aviv University, Ramat Aviv, Tel Aviv 69978, Israel.
Kelly Velonia
Davey Loos
Sadahiro Masuo
Mircea Cotlet
Yves Engelborghs
Johan Hofkens
Alan E Rowan
Roeland J M Nolte
Mark Van der Auweraer
Frans C de Schryver
Joseph Klafter
KU Leuven · BETel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single-molecule techniques offer a unique tool for studying the dynamical behavior of individual molecules and provide the possibility to construct distributions from individual events rather than from a signal stemming from an ensemble of molecules. In biological systems, known for their complexity, these techniques make it possible to gain insights into the detailed spectrum of molecular conformational changes and activities. Here, we report on the direct observation of a single lipase-catalyzed reaction for extended periods of time (hours), by using confocal fluorescence microscopy. When adding a profluorescent substrate, the monitored enzymatic activity appears as a trajectory of "on-state" and "off-state" events. The waiting time probability density function of the off state and the state-correlation function fit stretched exponentials, independent of the substrate concentration in a certain range. The data analysis unravels oscillations in the logarithmic derivative of the off-state waiting time probability density function and correlations between off-state events. These findings imply that the fluctuating enzyme model, which involves a spectrum of enzymatic conformations that interconvert on the time scale of the catalytic activity, best describes the observed enzymatic activity. Based on this model, values for the coupling and reaction rates are extracted.

Indexed as

Biophysical PhenomenaBiophysicsCandidaFungal ProteinsKineticsLipaseModels, BiologicalProtein ConformationThermodynamicsFungal ProteinsLipaselipase B, Candida antarctica

Identifiers

PMID15695587
PMCPMC548972
OpenAlexW2101263378

What OpenQuestion holds

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Registered trials

None linked

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.