Coupled molecular dynamics mediate long- and short-range epistasis between mutations that affect stability and aggregation kinetics [Biophysics and Computational Biology]

Multiple mutations are typically required to significantly improve protein stability or aggregation kinetics. However, when several substitutions are made in a single protein, the mutations can potentially interact in a nonadditive manner, resulting in epistatic effects, which can hamper protein-engineering strategies to improve thermostability or aggregation kinetics. Here, we have...

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