ArticleEuropean biophysics journal : EBJ2019
Thermodynamics of protein folding: methodology, data analysis and interpretation of data.
Article in European biophysics journal : EBJ, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.
What it found
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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.
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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.
Who cites it
6 citing papers in PubMed, 27 citations in OpenAlex.
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- Structural and functional effects of helix dipole moment in photoprotein Mnemiopsin 2.Scientific reports · 2025Article
- Pharmaceutical Analysis of Protein-Peptide Coformulations and the Influence of Polysorbates.Molecular pharmaceutics · 2025Article
- Article
- The Denaturant- and Mutation-Induced Disassembly ofMolecules (Basel, Switzerland) · 2022Article
- αα-hub coregulator structure and flexibility determine transcription factor binding and selection in regulatory interactomes.The Journal of biological chemistry · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermodynamics of protein folding refers to the stability measurements where structural changes of a given protein in the presence of a denaturing agent are monitored by spectroscopic or calorimetric techniques. In macroscopic point of view, protein stability represents the ratio of the population of its unfolded state to that of folded one in equilibrium condition, while in microscopic point of view, the stability is actually a net value from a combination of favorable and unfavorable contributions that affect the structural integrity of a protein molecule. In this manuscript, the principles and methodological aspects of thermodynamic studies and methods of data analysis as well as interpretation of the results are presented.
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Registered trials
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