ArticleJournal of the American Chemical Society2018
Thermodynamic Scale of β-Amino Acid Residue Propensities for an α-Helix-like Conformation.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Altered Intracellular Trafficking as a Mechanism for Prolonged Duration of G Protein-Coupled Receptor Activation.Journal of the American Chemical Society · 2026Article
- Prolonged signaling of backbone-modified glucagon-like peptide-Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Amino acid analogues provide multiple plausible pathways to prebiotic peptides.Journal of the Royal Society, Interface · 2024Review
- Effects of altered backbone composition on the folding kinetics and mechanism of an ultrafast-folding protein.Chemical science · 2024Article
- Effects of Replacing a Central Glycine Residue in GLP-1 on Receptor Affinity and Signaling Profile.Chembiochem : a European journal of chemical biology · 2023Article
- Differential Responses of the GLP-1 and GLP-2 Receptors to N-Terminal Modification of a Dual Agonist.Journal of the American Chemical Society · 2023Article
- Altered signaling at the PTH receptor via modified agonist contacts with the extracellular domain provides a path to prolonged agonism in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.Chemical science · 2022Article
- Structural and functional diversity among agonist-bound states of the GLP-1 receptor.Nature chemical biology · 2022Article
- Controlling the conformational stability of coiled-coil peptides with a single stereogenic center of a peripheral β-amino acid residue.RSC advances · 2022Article
- Impact of Substitution Registry on the Receptor-Activation Profiles of Backbone-Modified Glucagon-like Peptide-1 Analogues.Chembiochem : a European journal of chemical biology · 2019Article
- Coiled-Coil Peptide Beacon: A Tunable Conformational Switch for Protein Detection.Angewandte Chemie (International ed. in English) · 2018Article
- Receptor selectivity from minimal backbone modification of a polypeptide agonist.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Differential Effects of βAngewandte Chemie (International ed. in English) · 2018Article
Corrections and comments
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3 authors.
Funding
Abstract
A thiol-thioester exchange system has been used to measure the propensities of diverse β-amino acid residues to participate in an α-helix-like conformation. These measurements depend on formation of a parallel coiled-coil tertiary structure when two peptide segments become linked by thioester formation. One peptide segment contains a "guest" site that accommodates diverse β residues and is distal to the coiled-coil interface. We find that helix propensity is influenced by side chain placement within the β residue [β
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