Abstract
Designing protein sequences with a particular biological function is a long-lasting challenge for protein engineering. Recent advances in machine-learning-guided approaches focus on building a surrogate sequence-function model to reduce the burden of expensive in-lab experiments. In this paper, we study the exploration mechanism of model-guided sequence design. We leverage a natural property of protein fitness landscape that a concise set of mutations upon the wild-type sequence are usually sufficient to enhance the desired function. By utilizing this property, we propose Proximal Exploration (PEX) algorithm that prioritizes the evolutionary search for high-fitness mutants with low mutation counts. In addition, we develop a specialized model architecture, called Mutation Factorization Network (MuFacNet), to predict low-order mutational effects, which further improves the sample efficiency of model-guided evolution. In experiments, we extensively evaluate our method on a suite of in-silico protein sequence design tasks and demonstrate substantial improvement over baseline algorithms.
Original language | English (US) |
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Pages (from-to) | 18520-18536 |
Number of pages | 17 |
Journal | Proceedings of Machine Learning Research |
Volume | 162 |
State | Published - 2022 |
Externally published | Yes |
Event | 39th International Conference on Machine Learning, ICML 2022 - Baltimore, United States Duration: Jul 17 2022 → Jul 23 2022 |
ASJC Scopus subject areas
- Artificial Intelligence
- Software
- Control and Systems Engineering
- Statistics and Probability