Evidence map›Paper›PMID 22471784›Full record

ArticleJournal of the American Chemical Society2012

Minimalist probes for studying protein dynamics: thioamide quenching of selectively excitable fluorescent amino acids.

Jacob M Goldberg, Lee C Speight, Mark W Fegley, E James Petersson

Open access · greenAbstract 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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
8.2field-weighted citation impact, top 2% 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

34 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Continuous Histone Deacylase Activity Assays.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Fluorescently Labelled ATP Analogues for Direct Monitoring of Ubiquitin Activation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Minimalist IR and fluorescence probes of protein function.Current opinion in chemical biology · 2016
    Review
  19. 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 at 1 institution in 1 country.

Jacob M GoldbergDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA.
Lee C Speight
Mark W Fegley
E James Petersson
University of Pennsylvania · US

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Time-Of-Flight Instrument with Variable Ionization SourcesS10RR023444 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DMOCHOWSKI, IVAN JULIAN · 2007 to 2007
$308k
NCRR NIH HHS P41 RR001348NCRR NIH HHS P41RR001348NCRR NIH HHS S10 RR023444
6 · The paper itself

Abstract

Fluorescent probe pairs that can be selectively excited in the presence of Trp and Tyr are of great utility in studying conformational changes in proteins. However, the size of these probe pairs can restrict their incorporation to small portions of a protein sequence where their effects on secondary and tertiary structure can be tolerated. Our findings show that a thioamide bond-a single atom substitution of the peptide backbone-can quench fluorophores that are red-shifted from intrinsic protein fluorescence, such as acridone. Using steady-state and fluorescence lifetime measurements, we further demonstrate that this quenching occurs through a dynamic electron-transfer mechanism. In a proof-of-principle experiment, we apply this technique to monitor unfolding in a model peptide system, the villin headpiece HP35 fragment. Thioamide analogues of the natural amino acids can be placed in a variety of locations in a protein sequence, allowing one to make a large number of measurements to model protein folding.

Indexed as

AcridinesAcridonesAmino AcidsFluorescent DyesModels, MolecularMolecular ConformationOligonucleotide ProbesPeptidesProtein ConformationProtein DenaturationProtein FoldingProteinsProtein Structure, SecondaryProtein Structure, TertiarySpectrometry, FluorescenceThioamidesAcridinesacridoneAcridonesAmino AcidsFluorescent DyesOligonucleotide ProbesPeptidesProteinsThioamidesTryptophanTyrosine

Identifiers

PMID22471784
PMCPMC3360930
OpenAlexW1969733268

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.