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- W4211166801 abstract "Despite monumental advances in protein structure prediction, our ability to predict the effects of mutations on protein stability remains limited. Restricting our scope to solvent accessible mutation sites, we have developed an extremely fast method to calculate the relative stabilities of amino acid substitutions within a protein's structure using the structural data available in the Protein Data Bank. The stability of UBA(1), a small three-helix bundle, was successfully doubled from 2.4 to 4.8 kcal/mol using 4 solvent accessible mutations that were predicted with unprecedented physical accuracy (R2=0.97, slope=0.97)." @default.
- W4211166801 created "2022-02-13" @default.
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- W4211166801 date "2022-02-01" @default.
- W4211166801 modified "2023-09-26" @default.
- W4211166801 title "High accuracy achieved predicting stabilizing surface mutations in UBA(1)" @default.
- W4211166801 doi "https://doi.org/10.1016/j.bpj.2021.11.2492" @default.
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