ArticleProtein science : a publication of the Protein Society2004
Factors involved in the stability of isolated beta-sheets: Turn sequence, beta-sheet twisting, and hydrophobic surface burial.
Article in Protein science : a publication of the Protein Society, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 70 citations in OpenAlex.
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- Aromatic cluster mutations produce focal modulations of β-sheet structure.Protein science : a publication of the Protein Society · 2015Article
- Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.The journal of physical chemistry. B · 2011Article
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- How main-chains of proteins explore the free-energy landscape in native states.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Use of 13C(alpha) chemical shifts for accurate determination of beta-sheet structures in solution.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- A cross-strand Trp Trp pair stabilizes the hPin1 WW domain at the expense of function.Protein science : a publication of the Protein Society · 2007Article
- Cyclic modular beta-sheets.Journal of the American Chemical Society · 2007Article
- Bending elasticity of anti-parallel beta-sheets.Biophysical journal · 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
- Role of hydrophobic interactions and salt-bridges in beta-hairpin folding.Journal of molecular modeling · 2006Article
- Chemical shifts provide fold populations and register of beta hairpins and beta sheets.Journal of biomolecular NMR · 2005Article
- Folding cooperativity in a three-stranded beta-sheet model.Journal of molecular biology · 2005Article
- NMR structural analysis of a peptide mimic of the bridging sheet of HIV-1 gp120 in methanol and water.The Biochemical journal · 2005Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have recently reported on the design of a 20-residue peptide able to form a significant population of a three-stranded up-and-down antiparallel beta-sheet in aqueous solution. To improve our beta-sheet model in terms of the folded population, we have modified the sequences of the two 2-residue turns by introducing the segment DPro-Gly, a sequence shown to lead to more rigid type II' beta-turns. The analysis of several NMR parameters, NOE data, as well as Deltadelta(CalphaH), DeltadeltaC(beta), and Deltadelta(Cbeta) values, demonstrates that the new peptide forms a beta-sheet structure in aqueous solution more stable than the original one, whereas the substitution of the DPro residues by LPro leads to a random coil peptide. This agrees with previous results on beta-hairpin-forming peptides showing the essential role of the turn sequence for beta-hairpin folding. The well-defined beta-sheet motif calculated for the new designed peptide (pair-wise RMSD for backbone atoms is 0.5 +/- 0.1 A) displays a high degree of twist. This twist likely contributes to stability, as a more hydrophobic surface is buried in the twisted beta-sheet than in a flatter one. The twist observed in the up-and-down antiparallel beta-sheet motifs of most proteins is less pronounced than in our designed peptide, except for the WW domains. The additional hydrophobic surface burial provided by beta-sheet twisting relative to a "flat" beta-sheet is probably more important for structure stability in peptides and small proteins like the WW domains than in larger proteins for which there exists a significant contribution to stability arising from their extensive hydrophobic cores.
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