Redesign to Mechanism: Interpretable AI Reveals Determinants of Protein Hydrate Binding
mutations optimize the hydrophilic water ordering and hydrophobic anchoring. Val mutations further revealed two functional regions within the hydrate-binding site: an ordered anchoring region and a dynamic perturbation region. This work establishes an interpretable and generalizable framework for engineering high-performance AFPs.
Authors
- Junjie Liu (ORCID: https://orcid.org/0000-0002-6264-005X)
- Nan Zhang (ORCID: https://orcid.org/0000-0002-8097-6876)
- YJ Li
- Teer Ba (ORCID: https://orcid.org/0009-0008-2926-9579)
- Li-Rong Zhang
Institutions
- Inner Mongolia University (CN)
Publication Details
- Journal
- The Journal of Physical Chemistry Letters
- Published
- 2026-05-23
- DOI
- https://doi.org/10.1021/acs.jpclett.6c00954
- Primary Topic
- Machine Learning in Bioinformatics
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China