ReviewBiophysical chemistry2010
beta-hairpin-forming peptides; models of early stages of protein folding.
Review in Biophysical chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- De Novo Designed β-Hairpin Peptides Mimicking the Copper-Binding Histidine Brace Motif of Lytic Polysaccharide Monooxygenases.Angewandte Chemie (International ed. in English) · 2025Article
- Chameleon Sequences-Structural Effects in Proteins Characterized by Hydrophobicity Disorder.ACS omega · 2024Article
- A NovelBiology · 2021Article
- A systematic analysis of the beta hairpin motif in the Protein Data Bank.Protein science : a publication of the Protein Society · 2021Article
- Perspective Insights to Bio-Nanomaterials for the Treatment of Neurological Disorders.Frontiers in bioengineering and biotechnology · 2021Review
- Folding of Truncated Granulin Peptides.Biomolecules · 2020Article
- Mutation-induced change in chignolin stability from π-turn to α-turn.RSC advances · 2020Article
- Structures of single-layer β-sheet proteins evolved from β-hairpin repeats.Protein science : a publication of the Protein Society · 2019Article
- Halogen Bonding: A Powerful Tool for Modulation of Peptide Conformation.Biochemistry · 2017Article
- Assessing the Ability of Spectroscopic Methods to Determine the Difference in the Folding Propensities of Highly Similar β-Hairpins.ACS omega · 2017Article
- TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Biophysical journal · 2016Article
- Fragments of the V1/V2 domain of HIV-1 glycoprotein 120 engineered for improved binding to the broadly neutralizing PG9 antibody.Molecular immunology · 2016Article
- Molecular dynamics of protein A and a WW domain with a united-residue model including hydrodynamic interaction.The Journal of chemical physics · 2016Article
- Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptide.Scientific reports · 2015Article
- The impact of interchain hydrogen bonding on β-hairpin stability is readily predicted by molecular dynamics simulation.Biopolymers · 2015Article
- Amino acid distribution rules predict protein fold: protein grammar for beta-strand sandwich-like structures.Biomolecules · 2015Article
- Kinks, loops, and protein folding, with protein A as an example.The Journal of chemical physics · 2014Article
- Improvement of the treatment of loop structures in the UNRES force field by inclusion of coupling between backbone- and side-chain-local conformational states.Journal of chemical theory and computation · 2013Article
- Local vs global motions in protein folding.Journal of chemical theory and computation · 2013Article
- Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton model.Journal of biological physics · 2012Article
Corrections and comments
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4 authors.
Funding
Abstract
Formation of beta-hairpins is considered the initial step of folding of many proteins and, consequently, peptides constituting the beta-hairpin sequence of proteins (the beta-hairpin-forming peptides) are considered as models of early stages of protein folding. In this article, we discuss the results of experimental studies (circular-dichroism, infrared and nuclear magnetic resonance spectroscopy, and differential scanning calorimetry) of the structure of beta-hairpin-forming peptides excised from the B1 domain of protein G, which are known to fold on their own. We demonstrate that local interactions at the turn sequence and hydrophobic interactions between nonpolar residues are the dominant structure-determining factors, while there is no convincing evidence that stable backbone hydrogen bonds are formed in these peptides in aqueous solution. Consequently, the most plausible mechanism for folding of the beta-hairpin sequence appears to be the broken-zipper mechanism consisting of the following three steps: (i) bending the chain at the turn sequence owing to favorable local interactions, (ii) formation of loose hydrophobic contacts between nonpolar residues, which occur close to the contacts in the native structure of the protein but not exactly in the same position and, finally, (iii) formation of backbone hydrogen bonds and locking the hydrophobic contacts in the native positions as a hydrophobic core develops, sufficient to dehydrate the backbone peptide groups. This mechanism provides sufficient uniqueness (contacts form between residues that become close together because the chain is bent at the turn position) and robustness (contacts need not occur at once in the native positions) for folding a beta-hairpin sequence.
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