A Structural Landscape Depiction of Dynamic Stability Centers of Local Structure in Protein Thermostability Engineering.

Xu Qiu, Huan Liu, Peizhi Song, Xiaoran Cheng, Wanjing Wu, Siyang He, Weiwei Wang, Ping Xu, Hongzhi Tang

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Article in Research (Washington, D.C.), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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9 authors.

Xu QiuState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Huan LiuState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Peizhi SongState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Xiaoran ChengState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Wanjing WuState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Siyang HeState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Weiwei WangState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.

Ping XuState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.ORCID https://orcid.org/https://orcid.org/0000-0002-4418

Hongzhi TangState Key Laboratory of Microbial Metabolism and School of Life Sciences & Biotechnology, Shanghai Jiao Tong University, Shanghai 200240, P.R. China.ORCID https://orcid.org/https://orcid.org/0000-0002-7743

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Engineering protein thermostability is a key aspect of rational protein design, aiming to broaden the applicability of enzymes and enhance their industrial utility. In this study, we introduce a strategy for identifying and reinforcing dynamic stability centers of local structure (DSCLSs) to improve protein thermostability. A DSCLS comprises key structural residues and their interactions, representing the structural basis of protein stability. Molecular dynamics, cross-correlation amino acid networks, and other analytical techniques were integrated into the method. This approach was initially inspired by thermostability engineering of exodiol dioxygenases (EDOs). The method was validated through mutational analyses of mesophilic EDO MT-2, CpKR (ketoreductase from

Identifiers

PMID41498113

DOI10.34133/research.1054

PMCPMC12766707

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