Evidence map›Paper›PMID 24106309›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Nonequilibrium dynamics of helix reorganization observed by transient 2D IR spectroscopy.

Matthew J Tucker, Mohannad Abdo, Joel R Courter, Jianxin Chen, Stephen P Brown, Amos B Smith, Robin M Hochstrasser

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. 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. Article
  2. Protein Dynamics by Two-Dimensional Infrared Spectroscopy.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017
    Article
  12. The vibration of nanosprings affected by van der Waals interactions.Proceedings. Mathematical, physical, and engineering sciences · 2016
    Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Site-specific infrared probes of proteins.Annual review of physical chemistry · 2015
    Review
  18. Article
  19. Article
  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

7 authors.

Matthew J TuckerDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.
Mohannad Abdo
Joel R Courter
Jianxin Chen
Stephen P Brown
Amos B Smith
Robin M Hochstrasser

Funding

ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
NIGMS NIH HHS P41 GM104605NIGMS NIH HHS P41GM104605
6 · The paper itself

Abstract

The relaxation of helical structures very close to equilibrium is observed via transient 2D IR spectroscopy. An initial distribution of synthetically distorted helices having an unnatural bridge linking the 10th and 12th residues of an alanine-rich α-helix is released to evolve into the equilibrium distribution of α-helix conformations. The bridge constrains the structure to be slightly displaced from the full α-helix equilibrium near these residues, yet the peptide is not unfolded completely. The release is accomplished by a subpicosecond pulse of UV irradiation. The resulting 2D IR signals are used to obtain snapshots of the ∼100-ps helical conformational reorganization of the distorted dihedral angle and distance between amide units at chemical bond length-scale resolution. The decay rates of the angle between the dipoles, dihedral angles, and distance autocorrelations obtained from molecular dynamics simulations support the experiments, providing evidence that the final helix collapse conforms to linear response theory.

Indexed as

Molecular Dynamics SimulationProtein Structure, SecondaryAmino Acid SequenceKineticsModels, MolecularMolecular Sequence DataOligopeptidesPeptidesSpectrophotometry, InfraredSpectroscopy, Fourier Transform InfraredOligopeptidesPeptideshelix dynamicssynthetic peptidestetrazines

Identifiers

PMID24106309
PMCPMC3808647

What OpenQuestion holds

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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.