Evidence map›Paper›PMID 35271392›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Molten globule-like transition state of protein barnase measured with calorimetric force spectroscopy.

Marc Rico-Pasto, Annamaria Zaltron, Sebastian J Davis, Silvia Frutos, Felix Ritort

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

16 citing papers in PubMed, 40 citations in OpenAlex.

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  6. Universal cold RNA phase transitions.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

5 authors at 4 institutions in 3 countries.

Marc Rico-PastoSmall Biosystems Lab, Condensed Matter Physics Department, University of Barcelona, 08028 Barcelona, Spain.ORCID 0000-0003-0045-3379
Annamaria ZaltronPhysics and Astronomy Department, University of Padova, 35131 Padova, Italy.ORCID 0000-0002-5633-809X
Sebastian J DavisLaboratory of Nanoscale Biology, Institute of Bioengineering, School of Engineering, Ecole Polytechnique Federale de Lausanne, 1015 Lausanne, Switzerland.ORCID 0000-0002-7930-8125
Silvia FrutosSpliceBio, 08028 Barcelona, Spain.
Felix RitortSmall Biosystems Lab, Condensed Matter Physics Department, University of Barcelona, 08028 Barcelona, Spain.ORCID 0000-0002-4869-5003
Universitat de Barcelona · ESÉcole Polytechnique Fédérale de Lausanne · CHInstitut de Biologia Molecular de Barcelona · ESUniversity of Padua · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SignificanceUnderstanding the molecular forces driving the unfolded polypeptide chain to self-assemble into a functional native structure remains an open question. However, identifying the states visited during protein folding (e.g., the transition state between the unfolded and native states) is tricky due to their transient nature. Here, we introduce calorimetric force spectroscopy in a temperature jump optical trap to determine the enthalpy, entropy, and heat capacity of the transition state of protein barnase. We find that the transition state has the properties of a dry molten globule, that is, high free energy and low configurational entropy, being structurally similar to the native state. This experimental single-molecule study characterizes the thermodynamic properties of the transition state in funneled energy landscapes.

Indexed as

Bacterial ProteinsOptical TweezersProtein FoldingRibonucleasesSingle Molecule ImagingCalorimetryProtein ConformationProtein DenaturationThermodynamicsBacillus amyloliquefaciens ribonucleaseBacterial ProteinsRibonucleasesfoldingmolten globuleproteinthermodynamicstransition state

Identifiers

PMID35271392
PMCPMC8931224
OpenAlexW4220849499

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.