ArticleComputational and structural biotechnology journal2024
Osmolyte-induced protein stability changes explained by graph theory.
Article in Computational and structural biotechnology journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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.
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.
Who cites it
2 citing papers in PubMed.
- Interplay of protein fluctuation and associated water dynamics in osmolyte-induced stabilization.Biophysical journal · 2025Article
- Helix Folding in One Dimension: Effects of Proline Co-Solvent on Free Energy Landscape of Hydrogen Bond Dynamics in Alanine Peptides.Life (Basel, Switzerland) · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enhanced stabilization of protein structures via the presence of inert osmolytes is a key mechanism adopted both by physiological systems and in biotechnological applications. While the intrinsic stability of proteins is ultimately fixed by their amino acid composition and organization, the interactions between osmolytes and proteins together with their concentrations introduce an additional layer of complexity and in turn, a method of modulating protein stability. Here, we combined experimental measurements with molecular dynamics simulations and graph-theory-based analyses to predict the stabilizing/destabilizing effects of different kinds of osmolytes on proteins during heat-mediated denaturation. We found that (i) proteins in solution with stability-enhancing osmolytes tend to have more compact interaction networks than those assumed in the presence of destabilizing osmolytes; (ii) a strong negative correlation (R = -0.85) characterizes the relationship between the melting temperature
Identifiers
What OpenQuestion holds
Registered trials
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.