Evidence map›Paper›PMID 42793199›Full record

ArticleBiomolecules2026

pH-Dependent Stability and Cooperativity of Protein Unfolding from Differential Scanning Calorimetry Using FitFoldData.

Knarik Yeritsyan, Vladimir Uversky, Artem Badasyan

Abstract read
In one paragraph

Article in Biomolecules, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Knarik YeritsyanLaboratory of Organic Matter Physics, University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia.ORCID 0009-0006-4815-7279
Vladimir UverskyDepartment of Molecular Medicine, USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd., MDC07, Tampa, FL 33612, USA.ORCID 0000-0002-4037-5857
Artem BadasyanMaterials Research Laboratory, University of Nova Gorica, Vipavska 13, SI-5000 Nova Gorica, Slovenia.ORCID 0000-0003-0563-5403

Funding

The Slovenian Research and Innovation Agency P2-0412
6 · The paper itself

Abstract

Protein folding is highly sensitive to environmental conditions such as pH, which can influence internal hydrogen bonding and interactions with the solvent. In this study, we use our FitFoldData online tool to analyze published differential scanning calorimetry (DSC) data on the unfolding of four proteins measured across different pH values. For each dataset, we examine the fitted thermodynamic parameters, including the intrapeptide and peptide-solvent hydrogen-bonding energies (

Indexed as

Calorimetry, Differential ScanningProteinsProtein UnfoldingSoftwareHydrogen BondingHydrogen-Ion ConcentrationProtein StabilityThermodynamicsProteinsbiopolymer stabilityDSC data analysisfolding cooperativityhelix–coil transitionhydrogen bondingpH dependenceprotein foldingsolvent effects on foldingthermodynamic modelingZimm–Bragg model

Identifiers

PMID42793199
PMCPMC13604171

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.