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- W2912129449 abstract "In cells, proteins are embedded in a crowded environment that controls their properties via manifold avenues including weak protein-macromolecule interactions. A molecular level understanding of these quinary interactions and their contribution to protein stability, function, and localization in the cell is central to modern structural biology. Using a mutational analysis to quantify the energetic contributions of single amino acids to the stability of the ALS related protein superoxide dismutase I (SOD1) in mammalian cells, we show that quinary interactions destabilize SOD1 by a similar energetic offset for most of the mutants, but there are notable exceptions: Mutants that alter its surface properties can even lead to a stabilization of the protein in the cell as compared to the test tube. In conclusion, quinary interactions can amplify and even reverse the mutational response of proteins, being a key aspect in pathogenic protein misfolding and aggregation." @default.
- W2912129449 created "2019-02-21" @default.
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- W2912129449 date "2019-02-11" @default.
- W2912129449 modified "2023-10-12" @default.
- W2912129449 title "Stability Effect of Quinary Interactions Reversed by Single Point Mutations" @default.
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- W2912129449 doi "https://doi.org/10.1021/jacs.8b13025" @default.
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