ArticleBiochemistry2017
Heterochiral Knottin Protein: Folding and Solution Structure.
Article in Biochemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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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
10 citing papers in PubMed, 16 citations in OpenAlex.
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Chirality Effects in Peptide-Based Dynamic Combinatorial Chemistry.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Heterogeneous-Backbone Proteomimetic Analogues of Lasiocepsin, a Disulfide-Rich Antimicrobial Peptide with a Compact Tertiary Fold.ACS chemical biology · 2022Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- A twist in the road less traveled: The AMBER ff15ipq-m force field for protein mimetics.The Journal of chemical physics · 2020Article
- Proteomimetics as protein-inspired scaffolds with defined tertiary folding patterns.Nature chemistry · 2020Review
- Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation.Chembiochem : a European journal of chemical biology · 2019Article
- Heterogeneous-Backbone Foldamer Mimics of a Computationally Designed, Disulfide-Rich Miniprotein.Chembiochem : a European journal of chemical biology · 2019Article
- Xenoprotein engineering via synthetic libraries.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Foldamer Tertiary Structure through Sequence-Guided Protein Backbone Alteration.Accounts of chemical research · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Homochirality is a general feature of biological macromolecules, and Nature includes few examples of heterochiral proteins. Herein, we report on the design, chemical synthesis, and structural characterization of heterochiral proteins possessing loops of amino acids of chirality opposite to that of the rest of a protein scaffold. Using the protein Ecballium elaterium trypsin inhibitor II, we discover that selective β-alanine substitution favors the efficient folding of our heterochiral constructs. Solution nuclear magnetic resonance spectroscopy of one such heterochiral protein reveals a homogeneous global fold. Additionally, steered molecular dynamics simulation indicate β-alanine reduces the free energy required to fold the protein. We also find these heterochiral proteins to be more resistant to proteolysis than homochiral l-proteins. This work informs the design of heterochiral protein architectures containing stretches of both d- and l-amino acids.
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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.