ArticleJournal of the American Chemical Society2017
Helix Propensities of Amino Acid Residues via Thioester Exchange.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
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Who cites it
13 citing papers in PubMed.
- Modulating thermal folded stability and catalytic activity of aRSC advances · 2026Article
- Potent and biased agonists of class B1 GPCRs from a heterochiral design strategy.Nature chemistry · 2026Article
- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Precise recognition of benzonitrile derivatives with supramolecular macrocycle of phosphorylated cavitand by co-crystallization method.Nature communications · 2024Article
- Amino acid analogues provide multiple plausible pathways to prebiotic peptides.Journal of the Royal Society, Interface · 2024Review
- Effects of Replacing a Central Glycine Residue in GLP-1 on Receptor Affinity and Signaling Profile.Chembiochem : a European journal of chemical biology · 2023Article
- Light-Fueled Primitive Replication and Selection in Biomimetic Chemical Systems.Journal of the American Chemical Society · 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
- Structural and functional diversity among agonist-bound states of the GLP-1 receptor.Nature chemical biology · 2022Article
- Characteristics and therapeutic applications of antimicrobial peptides.Biophysics reviews · 2021Review
- Protein disorder-to-order transition enhances the nucleosome-binding affinity of H1.Nucleic acids research · 2020Article
- Thermodynamics of helix formation in small peptides of varying length in vacuo, in implicit solvent, and in explicit solvent.Journal of molecular modeling · 2018Article
- Thermodynamic Scale of β-Amino Acid Residue Propensities for an α-Helix-like Conformation.Journal of the American Chemical Society · 2018Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We describe the use of thioester exchange equilibria to measure the propensities of amino acid residues to participate in helical secondary structure at room temperature in the absence of denaturants. Thermally or chemically induced unfolding has previously been employed to measure α-helix propensities among proteinogenic α-amino acid residues, and quantitative comparison with precedents indicates that the thioester exchange system is reliable for residues that lack side chain charge. This system allows the measurement of α-helix propensities for d-α-amino acid residues and propensities of residues with nonproteinogenic backbones, such as those derived from a β-amino acid, to participate in an α-helix-like secondary structure.
Identifiers
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.