Outside Back Cover: Enhancing Cold Adaptation of Bidomain Amylases by High‐Throughput Computational Engineering (Angew. Chem. Int. Ed. 29/2025)
The cover art symbolizes the transformation of the mesophilic amylase psA (red) into its cold-adapted variant psA121 (cyan) through computational linker engineering. The central swirling motif reflects a shift in temperature adaptation, driven by increased interdomain separation between the catalytic domain and the carbohydrate-binding module. This visual captures how a simple change in linker sequence enables enhanced enzymatic activity at low temperatures by modifying the conformational dynamics of bidomain enzyme amylase, as described by Zhongyue J. Yang et al. in their Research Article (e202505991).
Authors
- Yaoyukun Jiang (ORCID: https://orcid.org/0000-0002-6424-2231)
- Ning Ding (ORCID: https://orcid.org/0000-0002-2345-3649)
- Wook Shin (ORCID: https://orcid.org/0000-0002-4004-2809)
- Zhongyue John Yang (ORCID: https://orcid.org/0000-0003-0395-6617)
- Qianzhen Shao (ORCID: https://orcid.org/0000-0002-7787-0966)
- Xinchun Ran (ORCID: https://orcid.org/0009-0001-5052-1758)
- Robbie Ge
Institutions
- Vanderbilt University (US)
Publication Details
- Journal
- Angewandte Chemie International Edition
- Published
- 2025-06-11
- DOI
- https://doi.org/10.1002/anie.202512250
- Primary Topic
- Peptidase Inhibition and Analysis
- Type
- article
- Field-Weighted Citation Impact
- 0.00