ArticlebioRxiv : the preprint server for biology2024
Structural and energetic analysis of stabilizing indel mutations.
Article in bioRxiv : the preprint server for biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Amino acid insertions and deletions (indels) are among the most common protein mutations and necessitate changes to a protein's backbone geometry. Examining how indels affect protein folding stability (and especially how indels can increase stability) can help reveal the role of backbone energetics on stability and introduce new protein engineering strategies. Tsuboyama et al. measured folding stability for 57,698 single amino acid insertion or deletion mutants in 405 small domains, and this analysis identified 103 stabilizing mutants (ΔΔG
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