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- W2912235431 abstract "A promising approach many have applied to increase protein stability is consensus sequence design. “Consensus sequences” are composed of the most frequent residue at each position in an alignment of extant sequences. While there have been many successful applications of consensus design, the generality and underlying mechanisms with which succeeds in producing folded, stable proteins are unclear. Here, we address these questions by designing consensus sequences for a set of seven globular protein families. We find that all seven consensus proteins adopt the archetypal folds of their respective protein families. Five of the seven consensus proteins show enhanced thermodynamic stabilities compared to natural homologues, with the other two showing near-average and above-average stabilities. All consensus proteins assayed for function maintain biological activities, showing variable effects on molecular recognition and steady-state catalysis activities. Constructing multiple consensus sequences from diverse families of proteins allows us to examine sequence features that impart unique properties, such as high stability, on consensus proteins. Comparisons of the sequence features of consensus proteins and the multiple sequence alignments from which they derive show striking increases in charged residues at weakly-conserved surface positions. Currently, we are examining how these sequence features contribute to the observed effects of consensus substitution on stability and function through site-directed mutagenesis, making chimeric proteins that introduce specific features of consensus protein into extant proteins. We are also comparing our consensus design strategy to other sequence-based strategies such as ancestral reconstruction and residue covariation-based approaches. For the homeodomain, we find that the high stability of the consensus sequence results neither from sequence differences at conserved positions, nor from differences in charged residues. Rather, the large stability increase for the consensus sequence seems to result from many small contributions from varied substitutions." @default.
- W2912235431 created "2019-02-21" @default.
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- W2912235431 date "2019-02-01" @default.
- W2912235431 modified "2023-10-17" @default.
- W2912235431 title "Investigating the Generality and Biophysical Underpinnings of Consensus Protein Stability Enhancement" @default.
- W2912235431 doi "https://doi.org/10.1016/j.bpj.2018.11.245" @default.
- W2912235431 hasPublicationYear "2019" @default.
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