ArticleProtein science : a publication of the Protein Society2010
Helicity of short E-R/K peptides.
Article in Protein science : a publication of the Protein Society, 2010. 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, 38 citations in OpenAlex.
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- Structure-Guided Design of Proteomimetics Targeting the SARS-CoV-2 S-RBD/hACE2 Interface.Journal of medicinal chemistry · 2026Article
- How Well Do Molecular Dynamics Force Fields Model Peptides: A Systematic Benchmark across Diverse Folding Behaviors.The journal of physical chemistry. B · 2026Article
- Mechanistic Insights into Unary Peptide-Membrane Interactions Enable Stable Encapsulation and Trigger-Responsive Peptidyl Liposomes.Journal of the American Chemical Society · 2026Article
- Myosin VI drives arrestin-independent internalization and signaling of GPCRs.Nature communications · 2024Article
- Comparative Analysis of Cyclization Techniques in Stapled Peptides: Structural Insights into Protein-Protein Interactions in a SARS-CoV-2 Spike RBD/hACE2 Model System.International journal of molecular sciences · 2023Article
- Metal-Promoted Higher-Order Assembly of Disulfide-Stapled Helical Barrels.Nanomaterials (Basel, Switzerland) · 2023Article
- α-Helix stabilization by co-operative side chain charge-reinforced interactions to phosphoserine in a basic kinase-substrate motif.The Biochemical journal · 2022Article
- The T850D Phosphomimetic Mutation in the Androgen Receptor Ligand Binding Domain Enhances Recruitment at Activation Function 2.International journal of molecular sciences · 2022Article
- Role of Helical Structure in MBP Immunodominant Peptides for Efficient IgM Antibody Recognition in Multiple Sclerosis.Frontiers in chemistry · 2022Article
- Membrane partitioning and lipid selectivity of the N-terminal amphipathic H0 helices of endophilin isoforms.Biochimica et biophysica acta. Biomembranes · 2021Article
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- Order and disorder-An integrative structure of the full-length human growth hormone receptor.Science advances · 2021Article
- ER/K-link-Leveraging a native protein linker to probe dynamic cellular interactions.Methods in enzymology · 2021Review
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- Determinants of Helix Formation for a Kv1.3 Transmembrane Segment inside the Ribosome Exit Tunnel.Journal of molecular biology · 2017Article
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- Characterization of long and stable de novo single alpha-helix domains provides novel insight into their stability.Scientific reports · 2017Article
- Using Kinetic Network Models To Probe Non-Native Salt-Bridge Effects on α-Helix Folding.The journal of physical chemistry. B · 2016Article
- Grid-based backbone correction to the ff12SB protein force field for implicit-solvent simulations.Journal of chemical theory and computation · 2015Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Understanding the secondary structure of peptides is important in protein folding, enzyme function, and peptide-based drug design. Previous studies of synthetic Ala-based peptides (>12 a.a.) have demonstrated the role for charged side chain interactions involving Glu/Lys or Glu/Arg spaced three (i, i + 3) or four (i, i + 4) residues apart. The secondary structure of short peptides (<9 a.a.), however, has not been investigated. In this study, the effect of repetitive Glu/Lys or Glu/Arg side chain interactions, giving rise to E-R/K helices, on the helicity of short peptides was examined using circular dichroism. Short E-R/K-based peptides show significant helix content. Peptides containing one or more E-R interactions display greater helicity than those with similar E-K interactions. Significant helicity is achieved in Arg-based E-R/K peptides eight, six, and five amino acids long. In these short peptides, each additional i + 3 and i + 4 salt bridge has substantial contribution to fractional helix content. The E-R/K peptides exhibit a strongly linear melt curve indicative of noncooperative folding. The significant helicity of these short peptides with predictable dependence on number, position, and type of side chain interactions makes them an important consideration in peptide design.
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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.