ArticleProtein science : a publication of the Protein Society2021
Cooperative hydrophobic core interactions in the β-trefoil architecture.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Engineering the kinetic stability of a β-trefoil protein by tuning its topological complexity.Frontiers in molecular biosciences · 2023Article
- Variable and Conserved Regions of Secondary Structure in the β-Trefoil Fold: Structure Versus Function.Frontiers in molecular biosciences · 2022Article
- The ubiquitous buried water in the beta-trefoil architecture contributes to the folding nucleus and ~20% of the folding enthalpy.Protein science : a publication of the Protein Society · 2021Article
- Cooperative hydrophobic core interactions in the β-trefoil architecture.Protein science : a publication of the Protein Society · 2021Article
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1 author.
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Abstract
Symmetric protein architectures have a compelling aesthetic that suggests a plausible evolutionary process (i.e., gene duplication/fusion) yielding complex architecture from a simpler structural motif. Furthermore, symmetry inspires a practical approach to computational protein design that substantially reduces the combinatorial explosion problem, and may provide practical solutions for structure optimization. Despite such broad relevance, the role of structural symmetry in the key area of hydrophobic core-packing cooperativity has not been adequately studied. In the present report, the threefold rotational symmetry intrinsic to the β-trefoil architecture is shown to form a geometric basis for highly-cooperative core-packing interactions that both stabilize the local repeating motif and promote oligomerization/long-range contacts in the folding process. Symmetry in the β-trefoil structure also permits tolerance towards mutational drift that involves a structural quasi-equivalence at several key core positions.
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