Evidence map›Paper›PMID 20133846›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Full distance-resolved folding energy landscape of one single protein molecule.

J Christof M Gebhardt, Thomas Bornschlögl, Matthias Rief

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 93 papers.

0numbers the graph read from it
0cells of the map it votes in
93citing 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

93 citing papers in PubMed.

  1. Review
  2. Review
  3. Hierarchical friction memory leads to subdiffusive configurational dynamics of fast-folding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  16. Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2022
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33 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

3 authors.

J Christof M GebhardtPhysik Department E22, Technische Universität München, James Franck Strasse, 85748 Garching, Germany.
Thomas Bornschlögl
Matthias Rief

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Kinetic bulk and single molecule folding experiments characterize barrier properties but the shape of folding landscapes between barrier top and native state is difficult to access. Here, we directly extract the full free energy landscape of a single molecule of the GCN4 leucine zipper using dual beam optical tweezers. To this end, we use deconvolution force spectroscopy to follow an individual molecule's trajectory with high temporal and spatial resolution. We find a heterogeneous energy landscape of the GCN4 leucine zipper domain. The energy profile is divided into two stable C-terminal heptad repeats and two less stable repeats at the N-terminus. Energies and transition barrier positions were confirmed by single molecule kinetic analysis. We anticipate that deconvolution sampling is a powerful tool for the model-free investigation of protein energy landscapes.

Indexed as

Protein FoldingAmino Acid SequenceBasic-Leucine Zipper Transcription FactorsBiophysical PhenomenaMicroscopy, Atomic ForceModels, MolecularMolecular Sequence DataOptical TweezersProteinsSaccharomyces cerevisiae ProteinsThermodynamicsBasic-Leucine Zipper Transcription FactorsGCN4 protein, S cerevisiaeProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID20133846
PMCPMC2836620

What OpenQuestion holds

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Registered trials

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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.