ArticleJournal of biomolecular NMR2001
13C(alpha) and 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides.
Article in Journal of biomolecular NMR, 2001. 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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Who cites it
21 citing papers in PubMed.
- Peptide-Based Supramolecular Hydrogels as Drug Delivery Agents: Recent Advances.Gels (Basel, Switzerland) · 2022Review
- Partial structure, dampened mobility, and modest impact of a His tag in the SARS-CoV-2 Nsp2 C-terminal region.European biophysics journal : EBJ · 2021Article
- Modeling the mechanism of CLN025 beta-hairpin formation.The Journal of chemical physics · 2017Article
- Predicting the redox state and secondary structure of cysteine residues using multi-dimensional classification analysis of NMR chemical shifts.Journal of biomolecular NMR · 2016Article
- Micelle-Triggered β-Hairpin to α-Helix Transition in a 14-Residue Peptide from a Choline-Binding Repeat of the Pneumococcal Autolysin LytA.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015Article
- Type I and II β-turns prediction using NMR chemical shifts.Journal of biomolecular NMR · 2014Article
- 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
- Structural characterization by NMR of a double phosphorylated chimeric peptide vaccine for treatment of Alzheimer's disease.Molecules (Basel, Switzerland) · 2013Article
- Structured pathway across the transition state for peptide folding revealed by molecular dynamics simulations.PLoS computational biology · 2011Article
- β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins.Journal of the American Chemical Society · 2011Article
- beta-hairpin-forming peptides; models of early stages of protein folding.Biophysical chemistry · 2010Review
- Sequence inversion and phenylalanine surrogates at the beta-turn enhance the antibiotic activity of gramicidin S.Journal of medicinal chemistry · 2010Article
- Therapeutic index of gramicidin S is strongly modulated by D-phenylalanine analogues at the beta-turn.Journal of medicinal chemistry · 2009Article
- Effects of side-chain orientation on the 13C chemical shifts of antiparallel beta-sheet model peptides.Journal of biomolecular NMR · 2007Article
- Design and NMR conformational study of a beta-sheet peptide based on Betanova and WW domains.Protein science : a publication of the Protein Society · 2006Article
- Chemical shifts provide fold populations and register of beta hairpins and beta sheets.Journal of biomolecular NMR · 2005Article
- Predicting 15N chemical shifts in proteins using the preceding residue-specific individual shielding surfaces from phi, psi i-1, and chi 1 torsion angles.Journal of biomolecular NMR · 2004Article
- 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
- Unblocked statistical-coil tetrapeptides in aqueous solution: quantum-chemical computation of the carbon-13 NMR chemical shifts.Journal of biomolecular NMR · 2003Article
- Turn stability in beta-hairpin peptides: Investigation of peptides containing 3:5 type I G1 bulge turns.Protein science : a publication of the Protein Society · 2003Article
Corrections and comments
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Authors and funding
3 authors.
Funding
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Abstract
Unravelling the factors that contribute to the formation and the stability of beta-sheet structure in peptides is a subject of great current interest. A beta-hairpin, the smallest beta-sheet motif, consists of two antiparallel hydrogen-bonded beta-strands linked by a loop region. We have performed a statistical analysis on protein beta-hairpins showing that the most abundant types of beta-hairpins, 2:2, 3:5 and 4:4, have characteristic patterns of 13C(alpha) and 13C(beta) conformational shifts, as expected on the basis of their phi and psi angles. This fact strongly supports the potential value of 13C(alpha) and 13C(beta) conformational shifts as a means to identify beta-hairpin motifs in peptides. Their usefulness was confirmed by analysing the patterns of 13C(alpha) and 13C(beta) conformational shifts in 13 short peptides, 10-15 residues long, that adopt beta-hairpin structures in aqueous solution. Furthermore, we have investigated their potential as a method to quantify beta-hairpin populations in peptides.
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