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• W4283735504 endingPage "4172" @default.
• W4283735504 startingPage "4172" @default.
• W4283735504 abstract "The β-sheet is one of the common protein secondary structures, and the aberrant aggregation of β-sheets is implicated in various neurodegenerative diseases. Cross-strand interactions are an important determinant of β-sheet stability. Accordingly, both diagonal and lateral cross-strand interactions have been studied. Surprisingly, diagonal cross-strand ion-pairing interactions have yet to be investigated. Herein, we present a systematic study on the effects of charged amino acid side-chain length on a diagonal ion-pairing interaction between carboxylate- and ammonium-containing residues in a β-hairpin. To this end, 2D-NMR was used to investigate the conformation of the peptides. The fraction folded population and the folding free energy were derived from the chemical shift data. The fraction folded population for these peptides with potential diagonal ion pairs was mostly lower compared to the corresponding peptide with a potential lateral ion pair. The diagonal ion-pairing interaction energy was derived using double mutant cycle analysis. The Asp2-Dab9 (Asp: one methylene; Dab: two methylenes) interaction was the most stabilizing (-0.79 ± 0.14 kcal/mol), most likely representing an optimal balance between the entropic penalty to enable the ion-pairing interaction and the number of side-chain conformations that can accommodate the interaction. These results should be useful for designing β-sheet containing molecular entities for various applications." @default.
• W4283735504 created "2022-07-01" @default.
• W4283735504 creator A5002532631 @default.
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• W4283735504 creator A5076289881 @default.
• W4283735504 creator A5076777831 @default.
• W4283735504 creator A5091328095 @default.
• W4283735504 date "2022-06-29" @default.
• W4283735504 modified "2023-10-05" @default.
• W4283735504 title "The Effects of Charged Amino Acid Side-Chain Length on Diagonal Cross-Strand Interactions between Carboxylate- and Ammonium-Containing Residues in a β-Hairpin" @default.
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• W4283735504 doi "https://doi.org/10.3390/molecules27134172" @default.
• W4283735504 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/35807421" @default.
• W4283735504 hasPublicationYear "2022" @default.
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