Evidence map›Paper›PMID 22873643›Full record

ArticleJournal of the American Chemical Society2012

Raising the speed limit for β-hairpin formation.

Caitlin M Davis, Shifeng Xiao, Daniel P Raleigh, R Brian Dyer

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Highly parallelizable path sampling with minimal rejections using asynchronous replica exchange and infinite swaps.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Article
  3. Article
  4. Granger Causality Analysis of Chignolin Folding.Journal of chemical theory and computation · 2022
    Article
  5. Article
  6. Article
  7. Modeling the mechanism of CLN025 beta-hairpin formation.The Journal of chemical physics · 2017
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Fast protein folding kinetics.Quarterly reviews of biophysics · 2014
    Review
  15. How quickly can a β-hairpin fold from its transition state?The journal of physical chemistry. B · 2014
    Article
  16. Article
  17. Article
  18. Article
  19. Microsecond folding experiments and simulations: a match is made.Physical chemistry chemical physics : PCCP · 2013
    Article
  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

4 authors.

Caitlin M DavisDepartment of Chemistry, Emory University, Atlanta, Georgia 30322, USA.
Shifeng Xiao
Daniel P Raleigh
R Brian Dyer

Funding

EARLY EVENTS IN PROTEIN FOLDINGR01GM053640 · NIGMS · UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB · PI DYER, RICHARD BRIAN · 1996 to 2022
$6.5M
NIGMS NIH HHS R01 GM053640NIGMS NIH HHS R01 GM53640
6 · The paper itself

Abstract

Understanding the folding of the β-hairpin is a crucial step in studying how β-rich proteins fold. We have studied CLN025, an optimized ten residue synthetic peptide, which adopts a compact, well-structured β-hairpin conformation. Formation of the component β-sheet and β-turn structures of CLN025 was probed independently using a combination of equilibrium Fourier transform infrared spectroscopy and laser-induced temperature jump coupled with time-resolved infrared and fluorescence spectroscopies. We find that CLN025 is an ultrafast folder due to its small free energy barrier to folding and that it exceeds the predicted speed limit for β-hairpin formation by an order of magnitude. We also find that the folding mechanism cannot be described by a simple two-state model, but rather is a heterogeneous process involving two independent parallel processes. Formation of stabilizing cross-strand hydrophobic interactions and turn alignment occur competitively, with relaxation lifetimes of 82 ± 10 and 124 ± 10 ns, respectively, at the highest probed temperature. The ultrafast and heterogeneous folding kinetics observed for CLN025 provide evidence for folding on a nearly barrierless free energy landscape, and recalibrate the speed limit for the formation of a β-hairpin.

Indexed as

Amino Acid MotifsAmino Acid SequenceHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularOligopeptidesProtein FoldingThermodynamicsOligopeptides

Identifiers

PMID22873643
PMCPMC3443077

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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.