The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Direct Coupling Analysis and The Attention Mechanism
Open accessPreprint — published as 10.1186/s12859-025-06062-y
Abstract
Proteins are involved in nearly all cellular functions, encompassing roles in transport, signaling, enzymatic activity, and more. Their functionalities crucially depend on their complex three-dimensional arrangement. For this reason, being able to predict their structure from the amino acid sequence has been and still is a phenomenal computational challenge that the introduction of AlphaFold solved with unprecedented accuracy. However, the inherent complexity of AlphaFold's architectures makes it challenging to understand the rules that ultimately shape the protein's predicted structure. This study investigates a single-layer unsupervised model based on the attention mechanism. More precisely, we explore a Direct Coupling Analysis (DCA) method that mimics the attention mechanism of several popular Transformer architectures, such as AlphaFold itself. The model's parameters, notably fewer than those in standard DCA-based algorithms, can be directly used for extracting structural determinants such as the contact map of the protein family under study. Additionally, the functional form of the energy function of the model enables us to deploy a multi-family learning strategy, allowing us to effectively integrate information across multiple protein families, whereas standard DCA algorithms are typically limited to single protein families. Finally, we implemented a generative version of the model using an autoregressive architecture, capable of efficiently generating new proteins in silico. The effectiveness of our Attention-Based DCA architecture is evaluated using different families of evolutionary-related proteins, whose structural data is sourced from the Pfam database.In this study, we introduce a shallow, unsupervised model designed to understand the self-attention layer within the Evoformer block of AlphaFold. We establish a method based on Direct Coupling Analysis (DCA), wherein the interaction tensor undergoes decomposition, leveraging the same structure employed in Transformer architectures. The model's parameters, notably fewer than those in standard DCA, are interpretable through an examination of the resulting attention matrices. These matrices enable the extraction of contact information, subsequently utilized for constructing the contact map of a protein family. Additionally, the self-attention decomposition in the DCA Hamiltonian form adopted here facilitates the definition of multi-family learning architecture, enabling the inference of parameter sets shared across diverse protein families. Finally, an autoregressive generative version of the model is implemented, capable of efficiently generating new proteins in silico. This generative model reproduces the summary statistics of the original protein family while concurrently inferring direct contacts in the tertiary structure of the protein. The effectiveness of our Attention-Based DCA architecture is evaluated using Multiple Sequence Alignments (MSAs) of varying lengths and depths, with structural data sourced from the Pfam database.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
Flagged first, then by citations
Research works printed but not linked: 21
- 10.1126/science.1219021 · DOI · Paper page
- 10.1038/nrg3414 · DOI · Paper page
- 2018, Reports on Progress in Physics, 81, 032601
- 10.1073/pnas.0805923106 · DOI · Paper page
- 10.1073/pnas.1111471108 · DOI · Paper page
- 2013, Physical Review E, 87, 012707
- 1985, A learning algorithm for boltzmann machines, Cognitive Science, 9, 147
- 10.1093/molbev/msy007 · DOI
- 2021, Nature Communications, 12, 5800
- Nambiar A , Liu S , Hopkins M , Heflin M , Maslov S , and Ritz A. Transforming the Language of Life: Transformer Neural Networks for Protein Prediction Tasks. Pages: 2020.06.15.153643 Section: New Results. 2020. · DOI
- Wolf T , Debut L , Sanh V , et al. Transformers: State-of-the-Art Natural Language Processing. In: Proceedings of the 2020 Conference on Empirical Methods in Natural Language Processing: System Demonstrations. Online: Association for Computational Linguistics, 2020:38–45. · DOI · Paper page
- Bhattacharya N , Thomas N , Rao R , et al. Single Layers of Attention Suffice to Predict Protein Contacts. preprint. Bioinformatics, 2020. · DOI
- Rao R , Liu J , Verkuil R , et al. MSA Transformer. Pages: 2021.02.12.430858 Section: New Results. 2021. · DOI · Paper page
- 10.7554/eLife.79854 · DOI
- 10.1093/bioinformatics/btm604 · DOI
- 10.1371/journal.pone.0028265 · DOI
- 10.1073/pnas.90.15.7195 · DOI
- 10.1126/science.1089427 · DOI
- Vig J , Madani A , Varshney LR , Xiong C , Socher R , and Rajani NF . BERTology Meets Biology: Interpreting Attention in Protein Language Models. 2021. · DOI · Paper page
- 10.1016/j.neucom.2021.03.091 · DOI · Paper page
- 2021, The language of proteins: NLP, machine learning & protein sequences, Computational and Structural Biotechnology Journal, 19, 1750, 10.1016/j.csbj.2021.03.022 · DOI
Metadata
- Authors
- Caredda, F., & Pagnani, A.
- Affiliations
- Politecnico di Torino (IT)
- Corresponding author
- Caredda, Francesco
- Venue
- BMC Bioinformatics
- Publisher
- openRxiv
- Published
- 2024-02-08
- Volume
- 26
- Issue
- 1
- Pages
- 41-41
- ISSN
- 1471-2105 (ISSN-L)
- PMC
- PMC11804077
- OpenAlex
- W4407194157
- Cited by
- 5
- References
- 1
- Citations by year
- 2026: 2 · 2025: 3
- FWCI
- 1.50
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by-nc-nd
- creativecommons.org/licenses/by/4.0/ (vor)
- Locations
- BMC Bioinformatics (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- Research Square (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- PORTO@Iris (submittedVersion, cc-by-nc-nd)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- European Commission (PE00000013)
- Ministero dell’Istruzione, dell’Università e della Ricerca (022TE5B7X, 2022TE5B7X, 11.10.2022, PE00000013)
- NextGenerationEU (PE00000013)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Machine Learning in Bioinformatics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- direct coupling analysis, attention mechanism, protein structure prediction, AlphaFold, unsupervised learning, protein contact maps, autoregressive models, protein families, energy function
- MeSH terms
- Algorithms, Models, Molecular, Protein Conformation, Proteins, Protein Folding, Computational Biology
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review