ArticleThe Journal of organic chemistry2025
Thioamides in C5 Hydrogen Bonds: Implications for Protein β-Strands.
Article in The Journal of organic chemistry, 2025. 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
2 citing papers in PubMed.
- α-Alkylated α-amino acids reduce the aggregation of unfolded peptides.RSC advances · 2026Article
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Though thioamides are considered weaker hydrogen-bond acceptors than oxoamides, recent calculations suggest that they can enhance hydrogen bonds within the backbone of individual β-strands. We confirm this prediction through spectroscopic analysis of minimal amino-acid models. Further, incorporation of thioamides into the backbone of β-hairpin models highlights opportunities to control β-strand stability.
Indexed as
Identifiers
What OpenQuestion holds
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.