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Effects of chain length and N-methylation on a cation-pi interaction in a beta-hairpin peptide

机译:链长和N-甲基化对β-发夹肽中阳离子-pi相互作用的影响

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摘要

The effects of N-methylation and chain length on a cation-pi interaction have been investigated within the context of a beta-hairpin peptide. Significant enhancement of the interaction and structural stabilization of the hairpin have been observed upon Lys methylation. Thermodynamic analysis indicates an increased entropic driving force for folding upon methylation of Lys residues. Comparison of lysine to analogues ornithine (Orn) and diami-nobutyric acid (Dab) indicates that lysine provides the strongest cation-pi interaction and also provides the most stable beta-hairpin due to a combination of side chain-side chain interactions and beta-sheet propensities. These studies have significance for the recognition of methylated lysine in histone proteins.
机译:在β-发夹肽的背景下,已经研究了N-甲基化和链长对阳离子-pi相互作用的影响。 Lys甲基化后已观察到发夹相互作用和结构稳定的显着增强。热力学分析表明,Lys残基甲基化后折叠时的熵驱动力增加。赖氨酸与类似物鸟氨酸(Orn)和二氨基丁酸(Dab)的比较表明,由于侧链-侧链相互作用和β-氨基苯甲酸的结合,赖氨酸提供最强的阳离子-pi相互作用,还提供最稳定的β-发夹结构。表的倾向。这些研究对于识别组蛋白中的甲基化赖氨酸具有重要意义。

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