ArticleProceedings of the National Academy of Sciences of the United States of America1993
Helix capping propensities in peptides parallel those in proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed.
- N-Terminal Amine Chemistry Influences α-Synuclein Interactions with Lipid Bilayers.Biochemistry · 2026Article
- Molecular dynamics study of the helix-to-disorder transition in short antimicrobial peptides from Urodacus yaschenkoi.European biophysics journal : EBJ · 2025Article
- Role of Copper and Zinc Ions in the Hydrolytic Degradation of Neurodegeneration-Related Peptides.Molecules (Basel, Switzerland) · 2025Article
- The Iconic α-Helix: From Pauling to the Present.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Capping motifs in antimicrobial peptides and their relevance for improved biological activities.Frontiers in chemistry · 2024Review
- Side-Chain Chemistry Governs Hierarchical Order of Charge-Complementary β-sheet Peptide Coassemblies.Angewandte Chemie (International ed. in English) · 2023Article
- Changes in α-Synuclein Posttranslational Modifications in an AAV-Based Mouse Model of Parkinson's Disease.International journal of molecular sciences · 2023Article
- Alpha synuclein post translational modifications: potential targets for Parkinson's disease therapy?Frontiers in molecular neuroscience · 2023Review
- Dissecting the stability determinants of a challenging de novo protein fold using massively parallel design and experimentation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- An N-capping asparagine-lysine-proline (NKP) motif contributes to a hybrid flexible/stable multifunctional peptide scaffold.Chemical science · 2022Article
- How important is the N-terminal acetylation of alpha-synuclein for its function and aggregation into amyloids?Frontiers in neuroscience · 2022Review
- Molecular mechanism of Mad1 kinetochore targeting by phosphorylated Bub1.EMBO reports · 2021Article
- Helix N-Cap Residues Drive the Acid Unfolding That Is Essential in the Action of the Toxin Colicin A.Biochemistry · 2019Article
- Understanding interactions of Citropin 1.1 analogues with model membranes and their influence on biological activity.Peptides · 2019Article
- Electronic and Steric Control of n→π* Interactions: Stabilization of the α-Helix Conformation without a Hydrogen Bond.Chembiochem : a European journal of chemical biology · 2019Article
- Structural Impact of Phosphorylation and Dielectric Constant Variation on Synaptotagmin's IDR.Biophysical journal · 2018Article
- The Impact of N-terminal Acetylation of α-Synuclein on Phospholipid Membrane Binding and Fibril Structure.The Journal of biological chemistry · 2016Article
- Sensing pH via p-cyanophenylalanine fluorescence: Application to determine peptide pKa and membrane penetration kinetics.Analytical biochemistry · 2015Article
- Review
- An engineered Axl 'decoy receptor' effectively silences the Gas6-Axl signaling axis.Nature chemical biology · 2014Article
1 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
Helix content of peptides with various uncharged nonaromatic amino acids at either the N-terminal or C-terminal position has been determined. The choice of N-terminal amino acid has a major effect on helix stability: asparagine is the best, glycine is very good, and glutamine is the worst helix-stabilizing amino acid at this position. The rank order of helix stabilization parallels the frequencies of these amino acids at the N-terminal boundary (N-cap) position of helices in proteins found by Richardson and Richardson [Richardson, J. S. & Richardson, D. C. (1988) Science 240, 1648-1652], and the N-terminal amino acid in a peptide composed of helix-forming amino acids may be considered as the N-cap residue. The choice of C-terminal amino acid has only a minor effect on helix stability. N-capping interactions may be responsible for the asymmetric distribution of helix content within a given peptide found by various workers. An acetyl group on the N-terminal alpha-amino function cancels the N-cap effect and the acetyl group is equivalent to N-terminal asparagine in an unacetylated peptide. Our results demonstrate a close relationship between the mechanisms of alpha-helix formation in peptides and in proteins.
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