Optimizing protein stability in vivo.

By Linda Foit, G. Morgan, Maximilian J Kern, Lenz Steimer, Annekathrin von Hacht, James R. Titchmarsh, S. Warriner, S. Radford, J. Bardwell. 2009

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Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldability (2014, methodology): “This approach was originally developed by Foit et al. 23 to evolve protein stability in vivo .”
Protein stability by number: high-throughput and statistical approaches to one of protein science’s most difficult problems (2011, unknown): “Recently, Bardwell and co-workers developed a system in which a protein of interest (POI) is inserted into a loop of TEM-1 b-lactamase, where it was hypothesized that lower-stability mutants of the POI would generally lead to greater degradation by cellular proteases [8 ].”
A de novo protein binding pair by computational design and directed evolution (2011, result): “…Prb variants are less stable than either the wild-type starting protein (PH1109) or the computationally designed Prb (Supplemental Figure S2), consistent with other studies indicating a trade-off between monomer stability and function (Foit et al., 2009; Hackel et al., 2008; Xu et al., 2002).”