ArticleJournal of the American Chemical Society2013
Protein-like tertiary folding behavior from heterogeneous backbones.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
What it found
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Who cites it
48 citing papers in PubMed.
- Manipulating the Unfolded State of a Folded Protein through Site-Specific Backbone Modification.Biochemistry · 2026Article
- Interplay between CChembiochem : a European journal of chemical biology · 2025Article
- Tackling Undruggable Targets with Designer Peptidomimetics and Synthetic Biologics.Chemical reviews · 2024Review
- Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024Article
- Probing effects of site-specific aspartic acid isomerization on structure and stability of GB1 through chemical protein synthesis.Protein science : a publication of the Protein Society · 2024Article
- Protein Backbone Alteration in Non-Hairpin β-Turns: Impacts on Tertiary Folded Structure and Folded Stability.Chembiochem : a European journal of chemical biology · 2023Article
- Chemical Shifts of Artificial Monomers Used to Construct Heterogeneous-Backbone Protein Mimetics in Random Coil and Folded States.Peptide science (Hoboken, N.J.) · 2023Article
- Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.Chemical science · 2022Article
- Intragenic compensation through the lens of deep mutational scanning.Biophysical reviews · 2022Review
- Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022Review
- Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold.ACS chemical biology · 2022Article
- Chiral, sequence-definable foldamer-derived macrocycles.Chemical science · 2021Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- An Unusually Rapid Protein Backbone Modification Stabilizes the Essential Bacterial Enzyme MurA.Biochemistry · 2020Article
- Proteomimetic Zinc Finger Domains with Modified Metal-binding β-Turns.Peptide science (Hoboken, N.J.) · 2020Article
- A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics.The Journal of chemical physics · 2020Article
- Increasing protein stability by engineering the n → π* interaction at the β-turn.Chemical science · 2020Article
- Proteomimetics as protein-inspired scaffolds with defined tertiary folding patterns.Nature chemistry · 2020Review
- Switched reaction specificity in polyesterases towards amide bond hydrolysis by enzyme engineering.RSC advances · 2019Article
- Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation.Chembiochem : a European journal of chemical biology · 2019Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Because proteins play vital roles in life, much effort has been invested in their mimicry by synthetic agents. One approach is to design unnatural backbone oligomers ("foldamers") that fold like natural peptides. Despite success in secondary structure mimicry by such species, protein-like tertiary folds remain elusive. A fundamental challenge underlying this task is the design of a sequence of side chains that will specify a complex tertiary folding pattern on an unnatural backbone. We report here a sequence-based approach to convert a natural protein with a compact tertiary fold to an analogue with a backbone composed of ~20% unnatural building blocks but folding behavior similar to that of the parent protein.
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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.