ArticleThe journal of physical chemistry letters2021
One Plus One Makes Three: Triangular Coupling of Correlated Amino Acid Mutations.
Article in The journal of physical chemistry letters, 2021. 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, 10 citations in OpenAlex.
- Article
- Benchmarking Free Energy Calculations: Analysis of Single and Double Mutations Across Two Simulation Software Platforms for Two Protein Systems.bioRxiv : the preprint server for biology · 2025Article
- Protein stability models fail to capture epistatic interactions of double point mutations.Protein science : a publication of the Protein Society · 2025Article
- Evolutionary sequence and structural basis for the distinct conformational landscapes of Tyr and Ser/Thr kinases.Nature communications · 2024Article
- Accurate protein stability predictions from homology models.Computational and structural biotechnology journal · 2023Article
- The Importance of Weakly Co-Evolving Residue Networks in Proteins is Revealed by Visual Analytics.Frontiers in bioinformatics · 2022Article
- Divergence in Dimerization and Activity of Primate APOBEC3C.Journal of molecular biology · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Correlated mutations have played a pivotal role in the recent success in protein fold prediction. Understanding nonadditive effects of mutations is crucial for altering protein structure, as mutations of multiple residues may change protein stability or binding affinity in a manner unforeseen by the investigation of single mutants. While the couplings between amino acids can be inferred from homologous protein sequences, the physical mechanisms underlying these correlations remain elusive. In this work we demonstrate that calculations based on the first-principles of statistical mechanics are capable of capturing the effects of nonadditivities in protein mutations. The identified thermodynamic couplings cover the short-range as well as previously unknown long-range correlations. We further explore a set of mutations in staphyloccocal nuclease to unravel an intricate interaction pathway underlying the correlations between amino acid mutations.
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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.