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• W2023591147 endingPage "14921" @default.
• W2023591147 startingPage "14917" @default.
• W2023591147 abstract "Cation−π interactions have been proposed to be important contributors to protein structure and function. In particular, these interactions have been suggested to provide significant stability at the solvent-exposed surface of a protein. We have investigated the magnitude of cation−π interactions between phenylalanine (Phe) and lysine (Lys), ornithine (Orn), and diaminobutanoic acid (Dab) in the context of an α-helix and have found that only the Phe···Orn interaction provides significant stability to the helix, stabilizing it by −0.4 kcal/mol. This interaction energy is in the same range as a salt bridge in an α-helix, and equivalent to the recently reported Trp···Arg interaction in an α-helix, despite the fact that Trp···guanidinium interactions have been proposed to be stronger than Phe···ammonium interactions. These results indicate that even the simplest cation−π interaction can provide significant stability to protein structure and demonstrate the subtle factors that can influence the observed interaction energies in designed systems." @default.
• W2023591147 created "2016-06-24" @default.
• W2023591147 creator A5012196056 @default.
• W2023591147 creator A5034116233 @default.
• W2023591147 creator A5055415786 @default.
• W2023591147 date "2002-11-22" @default.
• W2023591147 modified "2023-09-23" @default.
• W2023591147 title "Simple Cation−π Interaction between a Phenyl Ring and a Protonated Amine Stabilizes an α-Helix in Water" @default.
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• W2023591147 doi "https://doi.org/10.1021/ja026721a" @default.
• W2023591147 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12475333" @default.
• W2023591147 hasPublicationYear "2002" @default.
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