Evidence map›Paper›PMID 22822216›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Direct observation of kinetic traps associated with structural transformations leading to multiple pathways of S-layer assembly.

Seong-Ho Shin, Sungwook Chung, Babak Sanii, Luis R Comolli, Carolyn R Bertozzi, James J De Yoreo

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. A self-assembling surface layer flattens the cytokinetic furrow to aid cell division in an archaeon.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. In vitro investigation of protein assembly by combined microscopy and infrared spectroscopy at the nanometer scale.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Rotational dynamics and transition mechanisms of surface-adsorbed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Two-step crystallization and solid-solid transitions in binary colloidal mixtures.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  9. Article
  10. A bacterial surface layer protein exploits multistep crystallization for rapid self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. Article
  13. In vitro single-cell dissection revealing the interior structure of cable bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. S-layers: principles and applications.FEMS microbiology reviews · 2014
    Article
  19. Review
  20. Review
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

6 authors.

Seong-Ho ShinMolecular Foundry, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA.
Sungwook Chung
Babak Sanii
Luis R Comolli
Carolyn R Bertozzi
James J De Yoreo

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The concept of a folding funnel with kinetic traps describes folding of individual proteins. Using in situ Atomic Force Microscopy to investigate S-layer assembly on mica, we show this concept is equally valid during self-assembly of proteins into extended matrices. We find the S-layer-on-mica system possesses a kinetic trap associated with conformational differences between a long-lived transient state and the final stable state. Both ordered tetrameric states emerge from clusters of the monomer phase, however, they then track along two different pathways. One leads directly to the final low-energy state and the other to the kinetic trap. Over time, the trapped state transforms into the stable state. By analyzing the time and temperature dependencies of formation and transformation we find that the energy barriers to formation of the two states differ by only 0.7 kT, but once the high-energy state forms, the barrier to transformation to the low-energy state is 25 kT. Thus the transient state exhibits the characteristics of a kinetic trap in a folding funnel.

Indexed as

Models, MolecularProtein ConformationProtein FoldingAluminum SilicatesBacillaceaeBacterial ProteinsCryoelectron MicroscopyCrystallizationKineticsMembrane GlycoproteinsMicroscopy, Atomic ForcePolymersTemperatureTime FactorsAluminum SilicatesBacterial ProteinsMembrane GlycoproteinsmicaPolymersS-layer proteins

Identifiers

PMID22822216
PMCPMC3420203

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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.