ArticleProceedings of the National Academy of Sciences of the United States of America2009
Evaluating beta-turn mimics as beta-sheet folding nucleators.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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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
- ExploreTurns: A web tool for the exploration, analysis, and classification of beta turns and structured loops in proteins; application to beta-bulge and Schellman loops, Asx helix caps, beta hairpins, and other hydrogen-bonded motifs.Protein science : a publication of the Protein Society · 2025Article
- Effects of altered backbone composition on the folding kinetics and mechanism of an ultrafast-folding protein.Chemical science · 2024Article
- Stabilized cyclic peptides as modulators of protein-protein interactions: promising strategies and biological evaluation.RSC medicinal chemistry · 2023Review
- An amino-domino model described by a cross-peptide-bond Ramachandran plot defines amino acid pairs as local structural units.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Conversion of Hydroxyproline "Doubly Customizable Units" to Hexahydropyrimidines: Access to Conformationally Constrained Peptides.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
- Prognosis of Biomarker of Alzheimer's Disease in the Function of the Retina and Secondary Molecular Structure Variation of the Retina and Brain.International journal of Alzheimer's disease · 2023Article
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- Implications of the unfolded state in the folding energetics of heterogeneous-backbone protein mimetics.Chemical science · 2022Article
- Identification of novel functional mini-receptors by combinatorial screening of split-WW domains.Chemical science · 2022Article
- An Improved Turn Structure for Inducing β-Hairpin Formation in Peptides.Angewandte Chemie (International ed. in English) · 2021Article
- Analysis of folded structure and folding thermodynamics in heterogeneous-backbone proteomimetics.Methods in enzymology · 2021Review
- Sampling of the conformational landscape of small proteins with Monte Carlo methods.Scientific reports · 2020Article
- Proteomimetic Zinc Finger Domains with Modified Metal-binding β-Turns.Peptide science (Hoboken, N.J.) · 2020Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Post-Translational Backbone Engineering through Selenomethionine-Mediated Incorporation of Freidinger Lactams.Angewandte Chemie (International ed. in English) · 2018Article
- Protein stabilization by tuning the steric restraint at the reverse turn.Chemical science · 2018Article
- Ribosomal synthesis and folding of peptide-helical aromatic foldamer hybrids.Nature chemistry · 2018Article
- Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Chembiochem : a European journal of chemical biology · 2018Article
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12 authors.
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Abstract
Beta-turns are common conformations that enable proteins to adopt globular structures, and their formation is often rate limiting for folding. Beta-turn mimics, molecules that replace the i + 1 and i + 2 amino acid residues of a beta-turn, are envisioned to act as folding nucleators by preorganizing the pendant polypeptide chains, thereby lowering the activation barrier for beta-sheet formation. However, the crucial kinetic experiments to demonstrate that beta-turn mimics can act as strong nucleators in the context of a cooperatively folding protein have not been reported. We have incorporated 6 beta-turn mimics simulating varied beta-turn types in place of 2 residues in an engineered beta-turn 1 or beta-bulge turn 1 of the Pin 1 WW domain, a three-stranded beta-sheet protein. We present 2 lines of kinetic evidence that the inclusion of beta-turn mimics alters beta-sheet folding rates, enabling us to classify beta-turn mimics into 3 categories: those that are weak nucleators but permit Pin WW folding, native-like nucleators, and strong nucleators. Strong nucleators accelerate folding relative to WW domains incorporating all alpha-amino acid sequences. A solution NMR structure reveals that the native Pin WW beta-sheet structure is retained upon incorporating a strong E-olefin nucleator. These beta-turn mimics can now be used to interrogate protein folding transition state structures and the 2 kinetic analyses presented can be used to assess the nucleation capacity of other beta-turn mimics.
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