ArticleProtein science : a publication of the Protein Society2003
Turn stability in beta-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns.
Article in Protein science : a publication of the Protein Society, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
17 citing papers in PubMed.
- A Computational Perspective to Intermolecular Interactions and the Role of the Solvent on Regulating Protein Properties.Chemical reviews · 2025Review
- Design of Peptides that Fold and Self-Assemble on Graphite.Journal of chemical information and modeling · 2022Article
- A systematic analysis of the beta hairpin motif in the Protein Data Bank.Protein science : a publication of the Protein Society · 2021Article
- De novo design of transmembrane β barrels.Science (New York, N.Y.) · 2021Article
- The effect of turn residues on the folding and cell-penetrating activity of β-hairpin peptides and applications toward protein delivery.Peptide science (Hoboken, N.J.) · 2020Article
- Disulfide-Mediated β-Strand Dimers: Hyperstable β-Sheets Lacking Tertiary Interactions and Turns.Journal of the American Chemical Society · 2015Article
- Design of self-assembling peptide hydrogelators amenable to bacterial expression.Biomaterials · 2015Article
- Mutational effects on the folding dynamics of a minimized hairpin.Biochemistry · 2013Article
- Molecular requirements for sorting of the chemokine interleukin-8/CXCL8 to endothelial Weibel-Palade bodies.The Journal of biological chemistry · 2009Article
- Structure-function-folding relationship in a WW domain.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Minimization and optimization of designed beta-hairpin folds.Journal of the American Chemical Society · 2006Article
- Chemical shifts provide fold populations and register of beta hairpins and beta sheets.Journal of biomolecular NMR · 2005Article
- Hairpin folding rates reflect mutations within and remote from the turn region.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor.Protein science : a publication of the Protein Society · 2005Article
- Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.Protein science : a publication of the Protein Society · 2004Article
- Use of thiol-disulfide equilibria to measure the energetics of assembly of transmembrane helices in phospholipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Determination of membrane protein stability via thermodynamic coupling of folding to thiol-disulfide interchange.Protein science : a publication of the Protein Society · 2003Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The turn-forming ability of a series of three-residue sequences was investigated by substituting them into a well-characterized beta-hairpin peptide. The starting scaffold, bhpW, is a disulfide-cyclized 10-residue peptide that folds into a stable beta-hairpin with two antiparallel strands connected by a two-residue reverse turn. Substitution of the central two residues with the three-residue test sequences leads to less stable hairpins, as judged by thiol-disulfide equilibrium measurements. However, analysis of NMR parameters indicated that each molecule retains a significant folded population, and that the type of turn adopted by the three-residue sequence is the same in all cases. The solution structure of a selected peptide with a PDG turn contained an antiparallel beta-hairpin with a 3:5 type I + G1 bulge turn. Analysis of the energetic contributions of individual turn residues in the series of peptides indicates that substitution effects have significant context dependence, limiting the predictive power of individual amino acid propensities for turn formation. The most stable and least stable sequences were also substituted into a more stable disulfide-cyclized scaffold and a linear beta-hairpin scaffold. The relative stabilities remained the same, suggesting that experimental measurements in the bhpW context are a useful way to evaluate turn stability for use in protein design projects. Moreover, these scaffolds are capable of displaying a diverse set of turns, which can be exploited for the mimicry of protein loops or for generating libraries of reverse turns.
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.