Entropy-Driven Protein Allosteric Effect in Cells Highlights the Role of Solvation Water Molecules
cells. Mutations far away from the binding interface were introduced, which alter the affinity through allosteric effects. The results indicate that entropy contributes favorably to the allosteric effect in cellular contexts. This entropy-driven allosteric effect is also corroborated by molecular dynamics (MD) simulations, which underscore the significance of the protein solvation water. The crowded macromolecules help to restrain solvation water, and the release of these water molecules creates a positive entropic gain, which in turn generates an allosteric effect in cells.
Authors
- Xiaoxu Chen (ORCID: https://orcid.org/0009-0006-5230-3777)
- Lishan Yao (ORCID: https://orcid.org/0000-0003-1797-922X)
- Xiangfei Song (ORCID: https://orcid.org/0000-0002-1471-1175)
- Mengting Wang (ORCID: https://orcid.org/0009-0007-8417-2879)
- Xueying Zhang
- Yefei Wang
Institutions
- Energy Institute (GB)
- Chinese Academy of Sciences (CN)
- Shandong Lianxing Energy Group (China) (CN)
- Qingdao Institute of Bioenergy and Bioprocess Technology (CN)
- University of Chinese Academy of Sciences (CN)
Publication Details
- Journal
- The Journal of Physical Chemistry B
- Published
- 2026-04-07
- DOI
- https://doi.org/10.1021/acs.jpcb.6c01283
- Primary Topic
- Protein Structure and Dynamics
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Natural Science Foundation of China
- Natural Science Foundation of Shandong Province
- Taishan Scholar Project of Shandong Province
- QIBEBT United Foundation
- National Postdoctoral Program for Innovative Talents
- National Key Research and Development Program of China