Evidence map›Paper›PMID 11087856›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy.

D S Talaga, W L Lau, H Roder, J Tang, Y Jia, W F DeGrado, R M Hochstrasser

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing 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

84 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Nile Red Fluorescence: Where's the Twist?The journal of physical chemistry. B · 2024
    Article
  5. Article
  6. Article
  7. Theory and Analysis of Single-Molecule FRET Experiments.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Enzyme molecules in solitary confinement.Molecules (Basel, Switzerland) · 2014
    Review
  18. Article
  19. Review
  20. Article

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

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.

D S TalagaDepartments of Chemistry and Biophysics and Biochemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
W L Lau
H Roder
J Tang
Y Jia
W F DeGrado
R M Hochstrasser

Funding

ZN-INDUCED PEPTIDE FOLDINGP41RR001348 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1985 to 2011
$8.7M
Vibrational and Optical Probes of Electric Fields in ProteinsP01GM048130 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1993 to 2007
$7.3M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
Ultrafast Processing in Proteins and Other AssembliesR01GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 1985 to 2013
$3.5M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
ULTRAFAST PROCESSES IN PROTEINS AND OTHER ASSEMBLIESR37GM012592 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOCHSTRASSER, ROBIN MAIN · 1992 to 2001
$493k
EVENTS IN DNA 2 STRUCTURAL CHANGES BY TIME-RESOLVED IRF32GM018589 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI TALAGA, DAVID S · 1997 to 1999
–
NCRR NIH HHS P41 RR001348NIGMS NIH HHS F32 GM018589NIGMS NIH HHS GM12592NIGMS NIH HHS GM48130NIGMS NIH HHS GM54616NIGMS NIH HHS P01 GM048130NIGMS NIH HHS R01 GM012592NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM012592NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

We report single-molecule measurements on the folding and unfolding conformational equilibrium distributions and dynamics of a disulfide crosslinked version of the two-stranded coiled coil from GCN4. The peptide has a fluorescent donor and acceptor at the N termini of its two chains and a Cys disulfide near its C terminus. Thus, folding brings the two N termini of the two chains close together, resulting in an enhancement of fluorescent resonant energy transfer. End-to-end distance distributions have thus been characterized under conditions where the peptide is nearly fully folded (0 M urea), unfolded (7.4 M urea), and in dynamic exchange between folded and unfolded states (3.0 M urea). The distributions have been compared for the peptide freely diffusing in solution and deposited onto aminopropyl silanized glass. As the urea concentration is increased, the mean end-to-end distance shifts to longer distances both in free solution and on the modified surface. The widths of these distributions indicate that the molecules are undergoing millisecond conformational fluctuations. Under all three conditions, these fluctuations gave nonexponential correlations on 1- to 100-ms time scale. A component of the correlation decay that was sensitive to the concentration of urea corresponded to that measured by bulk relaxation kinetics. The trajectories provided effective intramolecular diffusion coefficients as a function of the end-to-end distances for the folded and unfolded states. Single-molecule folding studies provide information concerning the distributions of conformational states in the folded, unfolded, and dynamically interconverting states.

Indexed as

DNA-Binding ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceCysteineDisulfidesEnergy TransferFluorescence PolarizationFungal ProteinsGlassMicroscopy, ConfocalMolecular Sequence DataPeptidesProbabilityProtein FoldingProtein KinasesProtein Structure, SecondaryCysteineDisulfidesDNA-Binding ProteinsFungal ProteinsPeptidesProtein KinasesSaccharomyces cerevisiae ProteinsUrea

Identifiers

PMID11087856
PMCPMC27171

What OpenQuestion holds

Textmetadata
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.