Evidence map›Paper›PMID 20687689›Full record

ArticleThe Journal of chemical physics2010

Polymer translocation through alpha-hemolysin pore with tunable polymer-pore electrostatic interaction.

Chiu Tai Andrew Wong, M Muthukumar

Abstract read
In one paragraph

Article in The Journal of chemical physics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

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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

2 authors.

Chiu Tai Andrew WongDepartment of Polymer Science and Engineering, University of Massachusetts, Amherst, Massachusetts 01003, USA.
M Muthukumar

Funding

Modeling Macromolecular Transport through Protein Channels and NanoporesR01HG002776 · NHGRI · UNIVERSITY OF MASSACHUSETTS AMHERST · PI MUTHUKUMAR, MURUGAPPAN · 2003 to 2022
$5.3M
NHGRI NIH HHS R01 HG002776NHGRI NIH HHS R01HG002776
6 · The paper itself

Abstract

We have measured the ionic current blockages produced by single molecules of sodium poly(styrene sulfonate) passing through an alpha-hemolysin protein pore under an electric field. Most of the blockage events were composed of one or two blockage levels of ionic current. By analyzing the statistics of different event types for different polymer lengths, applied voltages, and pH conditions, we have identified the molecular mechanism behind the two-level blockages. Our analysis of the data shows that not all blockages are successful translocation events and the propensity of successful translocation can be tuned by pH gradients across the protein pore. We interpret our results as the change in protein-polymer interaction via protonation of charged amino acid residues of alpha-hemolysin pore. In addition, we have constructed a stochastic theory for polymer translocation through alpha-hemolysin pore with tunable polymer-pore interactions. The theoretical calculations capture many features observed in our experiments.

Indexed as

Static ElectricityAlgorithmsBiological TransportEntropyHemolysin ProteinsHydrogen-Ion ConcentrationModels, TheoreticalPolymersPorosityProbabilityProtonsStochastic ProcessesHemolysin ProteinsPolymersProtons

Identifiers

PMID20687689
PMCPMC2921442

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.