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首页> 外文期刊>Biochemistry >Effect of charged amino acid side chain length at non-hydrogen bonded strand positions on β-hairpin stability
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Effect of charged amino acid side chain length at non-hydrogen bonded strand positions on β-hairpin stability

机译：非氢键链位置带电氨基酸侧链长度对β-发夹稳定性的影响

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摘要

β-Sheets have been implicated in various neurological disorders, and ～20% of protein residues adopt a sheet conformation. Therefore, studies on the structural origin of sheet stability can provide fundamental knowledge with potential biomedical applications. Oppositely charged amino acids are frequently observed across one another in antiparallel β-sheets. Interestingly, the side chains of natural charged amino acids Asp, Glu, Arg, Lys have different numbers of hydrophobic methylenes linking the backbone to the hydrophilic charged functionalities. To explore the inherent effect of charged amino acid side chain length on antiparallel sheets, the stability of a designed hairpin motif containing charged amino acids with varying side chain lengths at non-hydrogen bonded positions was studied. Peptides with the guest position on the N-terminal strand and the C-terminal strand were investigated by NMR methods. The charged amino acids (Xaa) included negatively charged residues with a carboxylate group (Asp, Glu, Aad in increasing length), positively charged residues with an ammonium group (Dap, Dab, Orn, Lys in increasing length), and positively charged residues with a guanidinium group (Agp, Agb, Arg, Agh in increasing length). The fraction folded and folding free energy for each peptide were derived from the chemical shift deviation data. The stability of the peptides with the charged residues at the N-terminal guest position followed the trends: Asp > Glu > Aad, Dap < Dab < Orn ～ Lys, and Agb < Arg < Agh < Agp. The stability of the peptides with the charged residues at the C-terminal guest position followed the trends: Asp < Glu < Aad, Dap ～ Dab < Orn ～ Lys, and Agb < Arg ～ Agp < Agh. These trends were rationalized by thermodynamic sheet propensity and cross-strand interactions.
机译：β-Sheets与多种神经系统疾病有关，约20％的蛋白质残基具有薄片构象。因此，对薄片稳定性的结构起源的研究可以为潜在的生物医学应用提供基础知识。经常在反平行的β-折叠中彼此相反地观察到带相反电荷的氨基酸。有趣的是，天然带电氨基酸Asp，Glu，Arg，Lys的侧链具有不同数量的疏水性亚甲基，将主链连接至亲水性带电官能团。为了探索带电荷的氨基酸侧链长度对反平行片的内在影响，研究了设计的发夹基序的稳定性，该发夹基序包含在非氢键位置含带变化的侧链长度的带电荷氨基酸。通过NMR方法研究了在N末端链和C末端链上具有客体位置的肽。带电氨基酸（Xaa）包括带羧基的带负电荷的残基（长度增加的Asp，Glu，Aad），带铵基的带正电荷的残基（长度增加的Dap，Dab，Orn，Lys）和带正电荷的残基带有胍类（长度不断增加的Agp，Agb，Arg，Agh）。从化学位移偏差数据得出每种肽的折叠分数和折叠自由能。 N端客体带电荷残基的肽的稳定性遵循以下趋势：Asp> Glu> Aad，Dap

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