Evidence map›Paper›PMID 28254940›Full record

ArticleScience (New York, N.Y.)2017

Hidden dynamics in the unfolding of individual bacteriorhodopsin proteins.

Hao Yu, Matthew G W Siewny, Devin T Edwards, Aric W Sanders, Thomas T Perkins

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
13.5field-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

94 citing papers in PubMed, 226 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Silanes to Silatranes: Robust Functionalization for Single-Molecule Force Spectroscopy.Chembiochem : a European journal of chemical biology · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Studying Biomolecular Protein Complexes via Origami and 3D-Printed Models.International journal of molecular sciences · 2024
    Article
  15. Article
  16. Article
  17. Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024
    Review
  18. Quantifying a light-induced energetic change in bacteriorhodopsin by force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  19. Article
  20. Article

34 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Hao YuJILA, National Institute of Standards and Technology and University of Colorado, Boulder, CO 80309, USA.ORCID 0000-0003-1589-7781
Matthew G W SiewnyJILA, National Institute of Standards and Technology and University of Colorado, Boulder, CO 80309, USA.ORCID 0000-0001-7345-6971
Devin T EdwardsJILA, National Institute of Standards and Technology and University of Colorado, Boulder, CO 80309, USA.ORCID 0000-0002-2612-9561
Aric W SandersRadio Frequency Technology Division, National Institute of Standards and Technology, Boulder, CO 80305, USA.ORCID 0000-0003-3371-8054
Thomas T PerkinsJILA, National Institute of Standards and Technology and University of Colorado, Boulder, CO 80309, USA. tperkins@jila.colorado.edu.ORCID 0000-0003-4826-9490
National Institute of Standards and Technology · US

Funding

Predoctoral Training Molecular BiophysicsT32GM065103 · NIGMS · UNIVERSITY OF COLORADO AT BOULDER · PI FALKE, JOSEPH J · 2002 to 2021
$4.3M
NIGMS NIH HHS T32 GM065103
6 · The paper itself

Abstract

Protein folding occurs as a set of transitions between structural states within an energy landscape. An oversimplified view of the folding process emerges when transiently populated states are undetected because of limited instrumental resolution. Using force spectroscopy optimized for 1-microsecond resolution, we reexamined the unfolding of individual bacteriorhodopsin molecules in native lipid bilayers. The experimental data reveal the unfolding pathway in unprecedented detail. Numerous newly detected intermediates-many separated by as few as two or three amino acids-exhibited complex dynamics, including frequent refolding and state occupancies of <10 μs. Equilibrium measurements between such states enabled the folding free-energy landscape to be deduced. These results sharpen the picture of the mechanical unfolding of membrane proteins and, more broadly, enable experimental access to previously obscured protein dynamics.

Indexed as

Protein UnfoldingBacteriorhodopsinsLipid BilayersMicroscopy, Atomic ForceProtein Conformation, beta-StrandSingle Molecule ImagingBacteriorhodopsinsLipid Bilayers

Identifiers

PMID28254940
PMCPMC5436802
OpenAlexW2592966007

What OpenQuestion holds

Textmetadata
LicenceTDM
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.