ArticleJournal of the American Chemical Society2008
Probing the lower size limit for protein-like fold stability: ten-residue microproteins with specific, rigid structures in water.
Article in Journal of the American Chemical Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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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.
The trial behind it
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Who cites it
21 citing papers in PubMed, 41 citations in OpenAlex.
- Tunable CH/π Interactions within a Tryptophan Zipper Motif to Stabilize the Fold of Long β-Hairpin Peptides.ACS chemical biology · 2023Article
- Design and Engineering of Miniproteins.ACS bio & med chem Au · 2022Review
- A Conformationally Stable Acyclic β-Hairpin Scaffold Tolerating the Incorporation of Poorly β-Sheet-Prone Amino Acids.Chembiochem : a European journal of chemical biology · 2022Article
- Folding in Place: Design of β-Strap Motifs to Stabilize the Folding of Hairpins with Long Loops.The Journal of organic chemistry · 2021Article
- Mutation-induced change in chignolin stability from π-turn to α-turn.RSC advances · 2020Article
- Analysis of molecular dynamics simulations of 10-residue peptide, chignolin, using statistical mechanics: Relaxation mode analysis and three-dimensional reference interaction site model theory.Biophysics and physicobiology · 2019Review
- Aryl-aryl interactions in designed peptide folds: Spectroscopic characteristics and optimal placement for structure stabilization.Biopolymers · 2016Article
- A Miniature Protein Stabilized by a Cation-π Interaction Network.Journal of the American Chemical Society · 2016Article
- Investigating the role of chain and linker length on the catalytic activity of an HJournal of coordination chemistry · 2016Article
- Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide.Scientific reports · 2015Article
- Disulfide-Mediated β-Strand Dimers: Hyperstable β-Sheets Lacking Tertiary Interactions and Turns.Journal of the American Chemical Society · 2015Article
- An improved capping unit for stabilizing the ends of associated β-strands.FEBS letters · 2014Article
- Captides: rigid junctions between beta sheets and small molecules.Journal of peptide science : an official publication of the European Peptide Society · 2014Article
- Circular permutation of a WW domain: folding still occurs after excising the turn of the folding-nucleating hairpin.Journal of the American Chemical Society · 2014Article
- Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.RSC advances · 2013Article
- 13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues.Journal of biomolecular NMR · 2013Article
- Mutational effects on the folding dynamics of a minimized hairpin.Biochemistry · 2013Article
- Fluorescence of tryptophan in designed hairpin and Trp-cage miniproteins: measurements of fluorescence yields and calculations by quantum mechanical molecular dynamics simulations.The journal of physical chemistry. B · 2013Article
- Designed hairpin peptides interfere with amyloidogenesis pathways: fibril formation and cytotoxicity inhibition, interception of the preamyloid state.Biochemistry · 2011Article
- β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.Journal of the American Chemical Society · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Mutational optimization of two long-range interactions first observed in Ac-WINGKWT-NH2, (a) bifurcated H-bonding involving the threonine amide H(N) and side chain OH and the N-terminal acetyl carbonyl and (b) an H-bond between the entgegen-H(N) of the C-terminal amide and the indole ring of Trp6 that stabilizes a face-to-edge indole/indole interaction between Trp1 and Trp6, has afforded < or = 10 residue systems that yield a remarkably stable fold in water. Optimization was achieved by designing a hydrophobic cluster that sequesters these H-bonds from solvent exposure. The structures and extent of amide H/D exchange protection for CH3CH2CO-WI pGXWTGPS (p = D-Pro, X = Leu or Ile) were determined. These two systems are greater than 94% folded at 298 K (97.5% at 280 K) with melting temperatures > 75 degrees C. The fold appears to display minimal fluxionality; a well-converged NMR structure rationalizes all of the large structuring shifts observed, and we suggest that these designed constructs can be viewed as microproteins.
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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.