Evidence map›Paper›PMID 23572157›Full record

ArticleScientific reports2013

Single molecule unfolding and stretching of protein domains inside a solid-state nanopore by electric field.

Kevin J Freedman, S Raza Haq, Joshua B Edel, Per Jemth, Min Jun Kim

Abstract read
In one paragraph

Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Threading of Single Protein Molecules Through a Solid-State Nanopore.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  7. Article
  8. Solid-State Nanopores for Biomolecular Analysis and Detection.Advances in biochemical engineering/biotechnology · 2024
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  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

5 authors.

Kevin J FreedmanDepartment of Chemical and Biological Engineering, Drexel University, Philadelphia, PA 19104, USA.
S Raza Haq
Joshua B Edel
Per Jemth
Min Jun Kim

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Single molecule methods have provided a significantly new look at the behavior of biomolecules in both equilibrium and non-equilibrium conditions. Most notable are the stretching experiments performed by atomic force microscopes and laser tweezers. Here we present an alternative single molecule method that can unfold a protein domain, observed at electric fields greater than 10(6) V/m, and is fully controllable by the application of increasing voltages across the membrane of the pore. Furthermore this unfolding mechanism is characterized by measuring both the residence time of the protein within the nanopore and the current blockade. The unfolding data supports a gradual unfolding mechanism rather than the cooperative transition observed by classical urea denaturation experiments. Lastly it is shown that the voltage-mediated unfolding is a function of the stability of the protein by comparing two mutationally destabilized variants of the protein.

Indexed as

Protein Interaction Domains and MotifsProtein UnfoldingModels, MolecularNanoporesProtein ConformationProtein DenaturationProteinsProtein StabilityUreaProteinsUrea

Identifiers

PMID23572157
PMCPMC3622078

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.