mlsanityData to 7 Oct 2026

Reverse Distillation: Consistently Scaling Protein Language Model Representations

arXiv 2603.07710 ↗First posted 8 Mar 2026cs.LG q-bio.BMcited by 0

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Abstract (arXiv)

Unlike the predictable scaling laws in natural language processing and computer vision, protein language models (PLMs) scale poorly: for many tasks, models within the same family plateau or even decrease in performance, with mid-sized models often outperforming the largest in the family. We introduce Reverse Distillation, a principled framework that decomposes large PLM representations into orthogonal subspaces guided by smaller models of the same family. The resulting embeddings have a nested, Matryoshka-style structure: the first k dimensions of a larger model's embedding are exactly the representation from the smaller model. This ensures that larger reverse-distilled models consistently outperform smaller ones. A motivating intuition is that smaller models, constrained by capacity, preferentially encode broadly-shared protein features. Reverse distillation isolates these shared features and orthogonally extracts additional contributions from larger models, preventing interference between the two. On ProteinGym benchmarks, reverse-distilled ESM-2 variants outperform their respective baselines at the same embedding dimensionality, with the reverse-distilled 15 billion parameter model achieving the strongest performance. Our framework is generalizable to any model family where scaling challenges persist. Code and trained models are available at https://github.com/rohitsinghlab/plm_reverse_distillation.

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References · 12

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  11. 2024xTrimoPGLM: Unified 100B-Scale Pre-trained Transformer for Deciphering the Language of Proteincited by 49
  12. 2025Sculpting Subspaces: Constrained Full Fine-Tuning in LLMs for Continual Learningcited by 15

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