Stability Oracle: a structure-based graph-transformer framework for identifying stabilizing mutations

Nat Commun. 2024 Jul 23;15(1):6170. doi: 10.1038/s41467-024-49780-2.

Abstract

Engineering stabilized proteins is a fundamental challenge in the development of industrial and pharmaceutical biotechnologies. We present Stability Oracle: a structure-based graph-transformer framework that achieves SOTA performance on accurately identifying thermodynamically stabilizing mutations. Our framework introduces several innovations to overcome well-known challenges in data scarcity and bias, generalization, and computation time, such as: Thermodynamic Permutations for data augmentation, structural amino acid embeddings to model a mutation with a single structure, a protein structure-specific attention-bias mechanism that makes transformers a viable alternative to graph neural networks. We provide training/test splits that mitigate data leakage and ensure proper model evaluation. Furthermore, to examine our data engineering contributions, we fine-tune ESM2 representations (Prostata-IFML) and achieve SOTA for sequence-based models. Notably, Stability Oracle outperforms Prostata-IFML even though it was pretrained on 2000X less proteins and has 548X less parameters. Our framework establishes a path for fine-tuning structure-based transformers to virtually any phenotype, a necessary task for accelerating the development of protein-based biotechnologies.

MeSH terms

  • Algorithms
  • Computational Biology / methods
  • Models, Molecular
  • Mutation*
  • Neural Networks, Computer
  • Protein Conformation
  • Protein Engineering / methods
  • Protein Stability*
  • Proteins* / chemistry
  • Proteins* / genetics
  • Thermodynamics*

Substances

  • Proteins