Optimizing enzyme thermostability by combining multiple mutations using protein language model
Abstract Optimizing enzyme thermostability is essential for advancements in protein science and industrial applications. Currently, (semi‐)rational design and random mutagenesis methods can accurately identify single‐point mutations that enhance enzyme thermostability. However, complex epistatic int...
Saved in:
| Main Authors: | , , , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Wiley
2024-12-01
|
| Series: | mLife |
| Subjects: | |
| Online Access: | https://doi.org/10.1002/mlf2.12151 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|