ArticleJournal of the American Chemical Society2014
New charge-bearing amino acid residues that promote β-sheet secondary structure.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Structural impact of thioamide incorporation into a β-hairpin.RSC chemical biology · 2022Article
- A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of Poorly β-Sheet-Prone Amino Acids.Chembiochem : a European journal of chemical biology · 2022Article
- Host-Guest Induced Peptide Folding with Sequence-Specific Structural Chirality.Journal of the American Chemical Society · 2021Article
- Fine-tuning of lysine side chain modulates the activity of histone lysine methyltransferases.Scientific reports · 2020Article
- Molecular Recognition of Lipid II by Lantibiotics: Synthesis and Conformational Studies of Analogues of Nisin and Mutacin Rings A and B.The Journal of organic chemistry · 2019Article
- Protein stabilization by tuning the steric restraint at the reverse turn.Chemical science · 2018Article
- Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function.The Journal of biological chemistry · 2017Article
- Engineering β-sheets employingChemical science · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Proteinogenic amino acid residues that promote β-sheet secondary structure are hydrophobic (e.g., Ile or Val) or only moderately polar (e.g., Thr). The design of peptides intended to display β-sheet secondary structure in water typically requires one set of residues to ensure conformational stability and an orthogonal set, with charged side chains, to ensure aqueous solubility and discourage self-association. Here we describe new amino acids that manifest substantial β-sheet propensity, by virtue of β-branching, and also bear an ionizable group in the side chain.
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Registered trials
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