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• W4384201557 abstract "Point mutations can exert beneficial effects on proteins, including stabilization. The stabilizing effects of mutations are typically attributed to changes in free energy and residue interactions. However, these explanations lack detail and physical insights, which hinder the mechanistic study of protein stabilization and prevent accurate computational prediction of stabilizing mutations. Here, we investigate the physical mechanism underlying the enhanced thermostability of a Hygromycin B phosphotransferase mutant, Hph5. We find that the unpredictable mutation A118V induces rotation of F199, allowing it to establish an aromatic-aromatic interaction with W235. In contrast, the predictable mutation T246A acts through static hydrophobic interactions within the protein core. These discoveries were accelerated by a residue-coevolution-based theory, which links mutational effects to stability-associated local structures, providing valuable guidance for mechanistic exploration. The established workflow will benefit the development of accurate stability prediction programs and can be used to mine a protein stability database for undiscovered physical mechanisms." @default.
• W4384201557 created "2023-07-14" @default.
• W4384201557 creator A5033980715 @default.
• W4384201557 creator A5076867367 @default.
• W4384201557 date "2023-07-13" @default.
• W4384201557 modified "2023-10-13" @default.
• W4384201557 title "Understanding the Stabilization Mechanism of a Thermostable Mutant of Hygromycin B Phosphotransferase by Protein Sector-Guided Dynamic Analysis" @default.
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• W4384201557 doi "https://doi.org/10.1021/acsomega.3c00373" @default.
• W4384201557 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37521677" @default.
• W4384201557 hasPublicationYear "2023" @default.
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