ArticleProceedings of the National Academy of Sciences of the United States of America2010
Structural characterization of a beta-turn mimic within a protein-protein interface.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- The mass spectrometric intact transition epitope mapping method supports protein engineering of foldon trimer variants.Scientific reports · 2025Article
- Synthesis of Fusahexin and Characterization of a Natural β-Turn Dipeptide.The Journal of organic chemistry · 2025Article
- Synthesis of β,β-Dinaphthyl Amino Acids: Towards Molecular Gearing in Peptides and Mini-Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- β-Turn Induction by a Diastereopure Azepane-Derived Quaternary Amino Acid.The Journal of organic chemistry · 2023Article
- Protein Backbone Alteration in Non-Hairpin β-Turns: Impacts on Tertiary Folded Structure and Folded Stability.Chembiochem : a European journal of chemical biology · 2023Article
- High five! Methyl probes at five ring positions of phenylalanine explore the hydrophobic core dynamics of zinc finger miniproteins.Chemical science · 2021Article
- Secondary Structure of the Novel Myosin Binding Domain WYR and Implications within Myosin Structure.Biology · 2021Article
- Covalent Linkage and Macrocylization Preserve and Enhance Synergistic Interactions in Catalytic Amyloids.Chembiochem : a European journal of chemical biology · 2021Article
- Tryptophan Analogues with Fixed Side-Chain Orientation: Expanding the Scope.Chembiochem : a European journal of chemical biology · 2021Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- Traceless solid-phase synthesis and β-turn propensity of 1,3-thiazole-based peptidomimetics.RSC advances · 2020Article
- β-Turn Mimics by Chemical Ligation.Organic letters · 2020Article
- Directed C(spChemical science · 2019Article
- Proteomics for cancer drug design.Expert review of proteomics · 2019Article
- Mimicry of a β-Hairpin Turn by a Nonpeptidic Laterally Flexible Foldamer.Organic letters · 2018Article
- Protein stabilization by tuning the steric restraint at the reverse turn.Chemical science · 2018Article
- Diversity of Secondary Structure in Catalytic Peptides with β-Turn-Biased Sequences.Journal of the American Chemical Society · 2017Article
- Engineering β-sheets employingChemical science · 2016Article
- Towards "bionic" proteins: replacement of continuous sequences from HIF-1α with proteomimetics to create functional p300 binding HIF-1α mimics.Chemical communications (Cambridge, England) · 2016Article
- Cadmium-cysteine coordination in the BK inner pore region and its structural and functional implications.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
β-Turns are secondary structure elements not only exposed on protein surfaces, but also frequently found to be buried in protein-protein interfaces. Protein engineering so far considered mainly the backbone-constraining properties of synthetic β-turn mimics as parts of surface-exposed loops. A β-turn mimic, Hot═Tap, that is available in gram amounts, provides two hydroxyl groups that enhance its turn-inducing properties besides being able to form side-chain-like interactions. NMR studies on cyclic hexapeptides harboring the Hot═Tap dipeptide proved its strong β-turn-inducing capability. Crystallographic analyses of the trimeric fibritin-foldon/Hot═Tap hybrid reveal at atomic resolution how Hot═Tap replaces a βI'-turn by a βII'-type structure. Furthermore, Hot═Tap adapts to the complex protein environment by participating in several direct and water-bridged interactions across the foldon trimer interface. As building blocks, β-turn mimics capable of both backbone and side-chain mimicry may simplify the design of synthetic proteins.
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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 Socratic graph.