Evidence map›Paper›PMID 20000466›Full record

ArticleJournal of the American Chemical Society2010

Detection of a transient intermediate in a rapid protein folding process by solid-state nuclear magnetic resonance.

Kan-Nian Hu, Wai-Ming Yau, Robert Tycko

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Review
  2. Article
  3. Interplay between CChembiochem : a European journal of chemical biology · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Time-resolved solid state NMR of biomolecular processes with millisecond time resolution.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2022
    Review
  9. Article
  10. Article
  11. Article
  12. NbAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021
    Review
  13. Transiently structured head domains control intermediate filament assembly.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Advances in studying protein disorder with solid-state NMR.Solid state nuclear magnetic resonance · 2020
    Review
  18. Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Heterogeneity in the Folding of Villin Headpiece Subdomain HP36.The journal of physical chemistry. B · 2018
    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

3 authors.

Kan-Nian HuLaboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, USA.
Wai-Ming Yau
Robert Tycko

Funding

Investigations of Protein Folding by Solid State NMRZIADK029063 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI TYCKO, ROBERT · 2009 to 2011
$740k
Intramural NIH HHS ZIA DK029063
6 · The paper itself

Abstract

We describe the use of solid-state NMR spectroscopy to characterize a partially folded state of the 35-residue helical protein HP35 created by rapid freeze-quenching from a thermally unfolded state on the 10-20 micros time scale. Two-dimensional solid-state (13)C NMR spectra of (13)C-labeled HP35 in frozen glycerol/water solution exhibit two sets of signals, one corresponding to strongly unfolded protein molecules and the other to an ensemble of molecules having native helical secondary structure but incomplete tertiary structure. The NMR data indicate that secondary structure forms within the freeze-quenching time scale but that full folding involves a slower phase of structural annealing. The approximately 5 micros folding time observed in earlier studies of HP35 by time-resolved optical techniques may not represent the time scale for full folding.

Indexed as

Protein FoldingFreezingKineticsMagnetic Resonance SpectroscopyModels, MolecularNeurofilament ProteinsPeptide FragmentsProtein DenaturationProtein Structure, SecondaryProtein Structure, TertiaryNeurofilament ProteinsPeptide Fragmentsvillin headpiece subdomain peptide

Identifiers

PMID20000466
PMCPMC2805027

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.