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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Backbone conformational dependence of peptide acidity.
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Backbone conformational dependence of peptide acidity.

机译：肽酸度的骨架构象依赖性。

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摘要

Electrostatic interactions at the protein surface yield over a billion-fold range of amide hydrogen exchange rates. This range is equivalent to the maximal degree of attenuation in exchange rates that have been shown to occur for amides buried within the protein interior. Continuum dielectric analysis of Ala-Ala, Ala-Gly, Gly-Ala and trans-Pro-Ala peptide conformer acidities predicts that the relative orientation of the two neighboring peptide groups can account for a million-fold variation in hydroxide-catalyzed hydrogen exchange rates. As in previous protein studies, an internal dielectric value of 3 was found to be applicable to simple model peptides, presumably reflecting the short lifetime of the peptide anion intermediate. Despite the million-fold range in conformer acidities, the small differences in the experimental exchange rates for these peptides are accurately predicted. Ala-Ala conformers with an extended N-terminal residue and the C-terminal residue in the alpha conformation are predictedto account for over 60% of the overall hydrogen exchange reaction, despite constituting only 12% of the protein coil population.
机译：在蛋白质表面的静电相互作用产生超过十亿倍范围的酰胺氢交换速率。该范围相当于交换速率的最大衰减程度，交换速率的最大衰减程度已证明对于埋在蛋白质内部的酰胺会发生。连续电介质分析Ala-Ala，Ala-Gly，Gly-Ala和trans-Pro-Ala肽构象异构体酸度表明，两个相邻肽基团的相对取向可以解释氢氧化物催化的氢交换速率的百万倍变化。与以前的蛋白质研究一样，内部介电值为3可用于简单模型肽，大概反映了肽阴离子中间体的短寿命。尽管构象酸度范围为百万倍，但仍可以准确预测这些肽的实验交换率的微小差异。尽管仅占蛋白质线圈种群的12％，但具有扩展的N末端残基和C末端残基的Ala-Ala构象异构体预计占整个氢交换反应的60％以上。

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