ProtLingo: Efficient Protein Language Modeling via Conditional Memory and Expert Routing
- URL: http://arxiv.org/abs/2609.04793v1
- Date: Fri, 04 Sep 2026 06:46:42 GMT
- Title: ProtLingo: Efficient Protein Language Modeling via Conditional Memory and Expert Routing
- Abstract summary: Protein language models (PLMs) provide a scalable approach for modeling sequence-function relationships from unlabeled sequences.<n>We introduce ProtLingo, an efficient PLM framework that augments a pretrained single-sequence backbone with conditional local memory and sparse expert routing.<n>ProtLingo achieves competitive performance with a 150M-scale backbone, including strong parameter efficiency on mutation-effect prediction.
- Score: 39.80134572747517
- License: http://creativecommons.org/licenses/by/4.0/
- Abstract: Proteins perform diverse cellular functions, and even single amino-acid substitutions can alter stability, activity, or molecular interactions. Protein language models (PLMs) provide a scalable approach for modeling such sequence--function relationships from unlabeled sequences, but increasing the size of dense Transformer backbones often brings substantial computational cost without consistently improving mutation-sensitive prediction. We introduce ProtLingo, an efficient PLM framework that augments a pretrained single-sequence backbone with conditional local memory and sparse expert routing. ProtLingo maps contextual residue representations into route-specific discrete codes, composes centered local windows into latent $N$-gram addresses, and retrieves reusable residual signals associated with recurring local sequence contexts. In parallel, selected feed-forward blocks are upcycled into sparse Mixture-of-Experts layers with shared and routed experts, enabling residue-dependent computation while activating only a subset of parameters. Experiments on protein fitness prediction, FLIP benchmarks, and supervised contact prediction show that ProtLingo achieves competitive performance with a 150M-scale backbone, including strong parameter efficiency on mutation-effect prediction and preserved long-range structural representations.
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