Explaining how mutations affect AlphaFold predictions
Transformer models, neural networks that learn context by identifying relationships in sequential data, underpin many recent advances in artificial intelligence. Nevertheless, their inner workings are difficult to explain. Here, we find that a transformer model within the AlphaFold architecture uses simple, sparse patterns of amino acids to select protein conformations. To identify these patterns, we developed a straightforward algorithm called Conformational Attention Analysis Tool (CAAT). CAAT identifies amino acid positions that affect AlphaFold's predictions substantially when modified. These effects are corroborated by experiments in several cases. By contrast, modifying amino acids ignored by CAAT affects AlphaFold predictions less, regardless of experimental ground truth. Our results demonstrate that CAAT successfully identifies the positions of some amino acids important for protein structure prediction, narrowing the search space required to predict effective mutations and suggesting a framework that can be applied to other transformer-based neural networks.
Authors
- Suchetan Dontha
- Joseph F. Thole (ORCID: https://orcid.org/0000-0003-4342-8165)
- Parveen Sharma (ORCID: https://orcid.org/0000-0002-5534-2417)
- Matthew Coudron
- Brian F. Volkman (ORCID: https://orcid.org/0000-0002-6681-5179)
- Madeleine F Clore
- Lauren Porter
Institutions
- National Institutes of Health (US)
- National Institute of Standards and Technology (US)
- Medical College of Wisconsin (US)
- United States National Library of Medicine (US)
- National Heart, Lung, and Blood Institute (US)
- Joint Center for Quantum Information and Computer Science (US)
- University of Maryland, College Park (US)
Publication Details
- Journal
- bioRxiv (Cold Spring Harbor Laboratory)
- Published
- 2026-01-04
- DOI
- https://doi.org/10.64898/2025.12.30.697132
- Primary Topic
- Machine Learning in Bioinformatics
- Type
- article
- Field-Weighted Citation Impact
- 0.00