ArticleNature communications2021
Design of buried charged networks in artificial proteins.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Deep learning based design of buried hydrogen bond networks with HBDesigner.bioRxiv : the preprint server for biology · 2026Article
- Identification of coevolving positions by ancestral reconstruction.Communications biology · 2025Article
- Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I.Nature communications · 2024Article
- Advancing Synthetic Hydrogels through Nature-Inspired Materials Chemistry.Advanced materials (Deerfield Beach, Fla.) · 2024Review
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- Molecular Principles of Redox-Coupled Protonation Dynamics in Photosystem II.Journal of the American Chemical Society · 2022Article
- Electronic Polarization Is Essential for the Stabilization and Dynamics of Buried Ion Pairs in Staphylococcal Nuclease Mutants.Journal of the American Chemical Society · 2022Article
- De Novo Design of a Highly Stable Ovoid TIM Barrel: Unlocking Pocket Shape towards Functional Design.Biodesign research · 2022Article
- Resolving Chemical Dynamics in Biological Energy Conversion: Long-Range Proton-Coupled Electron Transfer in Respiratory Complex I.Accounts of chemical research · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Soluble proteins are universally packed with a hydrophobic core and a polar surface that drive the protein folding process. Yet charged networks within the central protein core are often indispensable for the biological function. Here, we show that natural buried ion-pairs are stabilised by amphiphilic residues that electrostatically shield the charged motif from its surroundings to gain structural stability. To explore this effect, we build artificial proteins with buried ion-pairs by combining directed computational design and biophysical experiments. Our findings illustrate how perturbation in charged networks can introduce structural rearrangements to compensate for desolvation effects. We validate the physical principles by resolving high-resolution atomic structures of the artificial proteins that are resistant towards unfolding at extreme temperatures and harsh chemical conditions. Our findings provide a molecular understanding of functional charged networks and how point mutations may alter the protein's conformational landscape.
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Registered trials
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