ArticleTetrahedron2012
Relationship between side-chain branching and stoichiometry in β(3)-peptide bundles.
Article in Tetrahedron, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Novel Materials From the Supramolecular Self-Assembly of Short Helical βFrontiers in chemistry · 2019Review
- Positive allostery in metal ion binding by a cooperatively folded β-peptide bundle.Journal of the American Chemical Society · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The stability and stoichiometry of β(3)-peptide bundles is influenced by side-chain identity. β(3)-peptides containing β(3)-homoleucine on one helical face assemble into octamers, whereas those containing β(3)-homovaline form tetramers. From a structural perspective, the side chains of β(3)-homoleucine and β(3)-homovaline differ in terms of both side-chain length and γ-carbon branching. To evaluate the extent to which these two parameters control β(3)-peptide bundle stoichiometry, we synthesized the β(3)-peptide Acid-3Y, which contains β(3)-homoisoleucine in place of β(3)-homoleucine or β(3)-homovaline. Acid-3Y assembles into a stable tetramer whose stability resembles that of the previously characterized Acid-VY tetramer. These results suggest that β(3)-peptide bundle stoichiometry is dominated by the presence or absence of γ-carbon branching on core side chains.
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Registered trials
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