Related Experiment Video
Updated: May 28, 2026

A Practical Guide to Phage- and Robotics-Assisted Near-Continuous Evolution
Published on: January 12, 2024
Navigating high-order protein fitness landscapes via deep learning on directed evolution trajectories
Chengzhi Song1,2, Liang Ma1,2, Lingfeng Xue1
1Center for Quantitative Biology and Peking-Tsinghua Center for Life Sciences, Academy for Advanced Interdisciplinary Studies, Peking University, Beijing 100871, China.
None:
Accurately predicting the fitness effects of high-order mutations is a grand challenge in understanding and engineering proteins. Existing models, including pretrained protein language models, struggle to capture the multiresidue interactions that govern these effects. Here, we introduce DENet, a deep learning framework that harnesses the rich comutation information within directed evolution (DE) trajectories to reconstruct high-resolution fitness landscapes for deciphering and engineering of complex protein variants. Applied to the cancer target KRAS, DENet-guided screening systematically identified high-order mutants with potent activities and uncovered hidden allosteric mechanisms. For MEK1, DENet nominated complex variants with >1,000-fold increased drug resistance, revealed synergistic tail mutations, and retrospectively identified over 75% of known clinical mutations, largely outperforming existing models. To broaden the framework's applicability, we developed an in silico strategy that simulates directed evolution to infer comutation information from widely available single-mutant datasets. DENet provides a quantitative framework for navigating complex fitness landscapes, uniting the rational engineering of multimutation proteins with the elucidation of their mechanisms and clinical implications.
More Related Videos
Related Concept Videos
Evolution of New Traits in Microbes
Gene Evolution - Fast or Slow?
In contrast, regions which code...
Gene Evolution - Fast or Slow?
In contrast, regions which code...
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Conservation of Protein Domains
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

