ArticleBiophysical journal2007
Coarse-grained strategy for modeling protein stability in concentrated solutions. III: directional protein interactions.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Protein Association in Solution: Statistical Mechanical Modeling.Biomolecules · 2023Review
- Comparison of Huggins Coefficients and Osmotic Second Virial Coefficients of Buffered Solutions of Monoclonal Antibodies.Polymers · 2021Article
- Evaluating the Effects of Hinge Flexibility on the Solution Structure of Antibodies at Concentrated Conditions.Journal of pharmaceutical sciences · 2019Article
- Article
- Confinement Effects on Carbon Dioxide Methanation: A Novel Mechanism for Abiotic Methane Formation.Scientific reports · 2017Article
- Coupling of isotropic and directional interactions and its effect on phase separation and self-assembly.The Journal of chemical physics · 2016Article
- Terminal supraparticle assemblies from similarly charged protein molecules and nanoparticles.Nature communications · 2014Article
- Reaching new levels of realism in modeling biological macromolecules in cellular environments.Journal of molecular graphics & modelling · 2013Review
- Competition between folding and aggregation in a model for protein solutions.The European physical journal. E, Soft matter · 2010Article
- The role of entropy and polarity in intermolecular contacts in protein crystals.Acta crystallographica. Section D, Biological crystallography · 2009Article
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Authors and funding
4 authors.
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Abstract
We extend our coarse-grained modeling strategy described in parts I and II of this investigation to account for nonuniform spatial distributions of hydrophobic residues on the solvent-exposed surfaces of native proteins. Within this framework, we explore how patchy surfaces can influence the solvent-mediated protein-protein interactions, and the unfolding and self-assembly behaviors of proteins in solution. In particular, we compare the equilibrium unfolding and self-assembly trends for three model proteins that share the same overall sequence hydrophobicity, but exhibit folded configurations with different solvent-exposed native-state surface morphologies. Our model provides new insights into how directional interactions can affect native-state protein stability in solution. We find that strongly-directional attractions between native molecules with patchy surfaces can help stabilize the folded conformation through the formation of self-assembled clusters. In contrast, native proteins with more uniform surfaces are destabilized by protein-protein attractions involving the denatured state. Finally, we discuss how the simulation results provide insights into the experimental solution behaviors of several proteins that display directional interactions in their native states.
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