arXiv:2607. 22314v1 Announce Type: new Abstract: Multiple Sequence Alignments (MSAs) provide protein language models with explicit evolutionary context, but their large depth makes subsampling unavoidable under limited token budgets.
arXiv:2602. 17330v5 Announce Type: replace-cross Abstract: Comparative analysis of adaptive immune repertoires at population scale is hampered by two practical bottlenecks: the near-quadratic cost of pairwise affinity evaluations and dataset imbalances that obscure clinically important minority clonotypes.
ProtLingo is a protein language modeling framework that enhances a pretrained single‑sequence Transformer backbone with conditional local memory and sparse expert routing. It maps residue representations into discrete codes, composes local windows into latent N‑gram addresses, and retrieves reusable residual signals for recurring sequence contexts. The model also converts selected feed‑forward blocks into sparse Mixture‑of‑Experts layers, allowing residue‑dependent computation while activating only a subset of parameters, achieving competitive performance on protein fitness prediction, FLIP benchmarks, and supervised contact prediction with a 150M‑parameter backbone.
arXiv:2607. 23518v1 Announce Type: new Abstract: The rapid evolution of generative models has unlocked new potentials in protein binder design, a pivotal task in structural biology, by facilitating end-to-end generation via joint sequence-structure modeling or hallucination.
arXiv:2507. 08920v4 Announce Type: replace-cross Abstract: We introduce AMix-1, a powerful protein foundation model built on Bayesian Flow Networks and empowered by a systematic training methodology, encompassing pretraining scaling laws, emergent capability analysis, in-context learning mechanism, and test-time scaling algorithm.
arXiv:2609.37675v1 Announce Type: new Abstract: Protein Language Models (PLMs) have made remarkable progress following scaling laws established in natural language processing across sequence- and str...
arXiv:2606. 02386v1 Announce Type: new Abstract: Protein language models (PLMs) are passive oracles: they generate sequences in a single forward pass with no mechanism to consult external biophysical feedback or redirect generation when a candidate violates thermodynamic or structural constraints.
arXiv:2603. 14717v2 Announce Type: replace Abstract: Generating novel protein sequences that respect a family's statistical constraints typically requires training deep generative models on thousands to millions of examples.
SymFold introduces a symmetric dual‑path architecture that combines protein language models (PLMs) and multimodal protein language models (MPLMs) to iteratively guide protein sequence generation for inverse folding. By leveraging pretrained sequence evolution knowledge from PLMs and structural knowledge from MPLMs, the method improves upon the traditional serial pipeline where structure encoders produce coarse sequences refined by PLMs. Experiments on standard inverse‑folding benchmarks show state‑of‑the‑art performance, and ablation studies confirm the effectiveness of the symmetric design.
The paper investigates how guided protein language models can collapse onto off‑manifold representations when heavily steered to optimize a property. This collapse causes generated sequences to become low‑complexity and statistically similar to random amino‑acid input, yet the property oracle may still rate them highly. The authors propose a cheap, training‑free Mahalanobis filtering step that removes such off‑manifold candidates, improving both property scores and structural plausibility without altering the generator.
arXiv:2605. 02937v2 Announce Type: replace-cross Abstract: Deep learning in de novo protein design has achieved atomic-level fidelity.
arXiv:2606. 08100v1 Announce Type: new Abstract: Multimodal $\Delta\Delta G$ predictors integrating protein language models with inverse-folding representations achieve strong in-distribution accuracy on the Megascale dataset but exhibit limited robustness on out-of-distribution (OOD) proteins, persistent forward-reverse bias on paired-mutation benchmarks, and under-representation of rare stabilizing mutations.
arXiv:2606. 26578v1 Announce Type: new Abstract: Automating optimization modeling from natural language with large language models (LLMs) faces two key challenges.