ArticleScientific reports2019
Protein tertiary structure and the myoglobin phase diagram.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Deep mutational scanning reveals a de novo disulfide bond and combinatorial mutations for engineering thermostable myoglobin.Protein science : a publication of the Protein Society · 2025Article
- Review
- Dietary Heme-Containing Proteins: Structures, Applications, and Challenges.Foods (Basel, Switzerland) · 2022Review
- Exploring Structural Flexibility and Stability of α-Synuclein by the Landau-Ginzburg-Wilson Approach.The journal of physical chemistry. B · 2022Article
- Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics.Journal of chemical theory and computation · 2021Article
- On topology and knotty entanglement in protein folding.PloS one · 2021Article
- New Insights into Folding, Misfolding, and Nonfolding Dynamics of a WW Domain.The journal of physical chemistry. B · 2020Article
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Authors and funding
3 authors.
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Abstract
We develop an effective theory approach to investigate the phase properties of globular proteins. Instead of interactions between individual atoms or localized interaction centers, the approach builds directly on the tertiary structure of a protein. As an example we construct the phase diagram of (apo)myoglobin with temperature (T) and acidity (pH) as the thermodynamical variables. We describe how myoglobin unfolds from the native folded state to a random coil when temperature and acidity increase. We confirm the presence of two molten globule folding intermediates, and we predict an abrupt transition between the two when acidity changes. When temperature further increases we find that the abrupt transition line between the two molten globule states terminates at a tricritical point, where the helical structures fade away. Our results also suggest that the ligand entry and exit is driven by large scale collective motions that destabilize the myoglobin F-helix.
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