# A survey of downstream applications of evolutionary scale modeling protein language models

**Authors:** Qingyu Yang, Jiale Yu, Jie Zheng

PMC · DOI: 10.1002/qub2.70013 · Quantitative Biology · 2025-09-21

## TL;DR

This survey reviews how evolutionary scale modeling (ESM) protein language models are being used in protein science and engineering.

## Contribution

The paper provides a focused and comprehensive survey of ESM's latest developments and applications.

## Key findings

- ESM models capture mutation and conservation patterns in protein sequences effectively.
- Approximately 100 papers were analyzed to highlight ESM's impact on protein research.
- The survey discusses strengths and limitations of ESM for future applications.

## Abstract

The evolutionary scale modeling (ESM) series is promising to revolutionize protein science and engineering through large language models (LLMs), providing a robust framework for understanding the relationships among sequences, structures, and functions of proteins. Trained on a large number of unlabeled protein sequences, ESM models are able to capture intricate patterns of mutation and conservation, yielding insights into the structural and functional properties of proteins. Despite a growing body of literature surrounding ESM, existing surveys often fail to comprehensively describe its advancements or applications in a focused manner. This survey covers the latest developments of ESM, categorizing them into techniques of using ESM and downstream applications. Approximately 100 papers are selected and analyzed, highlighting recognized and innovative studies that exemplify the impact of ESM. Furthermore, we critically discuss the strengths and limitations of ESM to envision future applications. This review provides a valuable resource for researchers seeking to explore the power of ESM models and the emerging applications of LLMs in biology and medicine.

## Full text

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## Figures

3 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12806033/full.md

## References

157 references — full list in the complete paper: https://tomesphere.com/paper/PMC12806033/full.md

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Source: https://tomesphere.com/paper/PMC12806033