ArticleProceedings of the National Academy of Sciences of the United States of America2014
Effects of side chains in helix nucleation differ from helix propagation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Sequence Programmable Order-Disorder Transitions in Supramolecular Assembly of Peptide Nanofibers.Journal of the American Chemical Society · 2025Article
- Single-Molecule Electrical Profiling of Peptides and Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Review
- Inhibition of Aurora-A/N-Myc Protein-Protein Interaction Using Peptidomimetics: Understanding the Role of Peptide Cyclization.Chembiochem : a European journal of chemical biology · 2024Article
- Macrocyclic β-Sheets Stabilized by Hydrogen Bond Surrogates.Angewandte Chemie (International ed. in English) · 2023Article
- α-Helix stabilization by co-operative side chain charge-reinforced interactions to phosphoserine in a basic kinase-substrate motif.The Biochemical journal · 2022Article
- Bent Into Shape: Folded Peptides to Mimic Protein Structure and Modulate Protein Function.Peptide science (Hoboken, N.J.) · 2020Article
- Exposing the Nucleation Site in α-Helix Folding: A Joint Experimental and Simulation Study.The journal of physical chemistry. B · 2019Article
- Hydrogen Bond Surrogate Stabilization of β-Hairpins.ACS chemical biology · 2018Article
- Probing Charge Transport through Peptide Bonds.The journal of physical chemistry letters · 2018Article
- Microscopic nucleation and propagation rates of an alanine-based α-helix.Physical chemistry chemical physics : PCCP · 2017Article
- Populations of the Minor α-Conformation in AcGXGNH2 and the α-Helical Nucleation Propensities.Scientific reports · 2016Article
- Hydrocarbon constrained peptides - understanding preorganisation and binding affinity.Chemical science · 2016Article
- An optimal hydrogen-bond surrogate for α-helices.Chemical communications (Cambridge, England) · 2016Article
- Effects of conformational ordering on protein/polyelectrolyte electrostatic complexation: ionic binding and chain stiffening.Scientific reports · 2016Article
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Authors and funding
4 authors.
Funding
Abstract
Helix-coil transition theory connects observable properties of the α-helix to an ensemble of microstates and provides a foundation for analyzing secondary structure formation in proteins. Classical models account for cooperative helix formation in terms of an energetically demanding nucleation event (described by the σ constant) followed by a more facile propagation reaction, with corresponding s constants that are sequence dependent. Extensive studies of folding and unfolding in model peptides have led to the determination of the propagation constants for amino acids. However, the role of individual side chains in helix nucleation has not been separately accessible, so the σ constant is treated as independent of sequence. We describe here a synthetic model that allows the assessment of the role of individual amino acids in helix nucleation. Studies with this model lead to the surprising conclusion that widely accepted scales of helical propensity are not predictive of helix nucleation. Residues known to be helix stabilizers or breakers in propagation have only a tenuous relationship to residues that favor or disfavor helix nucleation.
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