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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model
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The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model

机译：pH依赖的葡萄球菌核酸酶稳定性与三态变性模型不兼容

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摘要

Six single substitution mutations, V66F, V66G, V66N, V66Q, V66S, V66T, and V66Y, were made in the background of a highly stable triple mutant (P117G, H124L, and S128A) of staphylococcal nuclease. The thermodynamic stabilities of wild type staphylococcal nuclease, of the stable triple mutant and of its six variants were determined by guanidine hydrochloride denaturation in thirteen different buffers spanning the pH range 4.5 to 10.2. Within experimental error the values of DELTAG(H_2o) and m_(GuCl) for the various proteins measured over this wide range of pH maintain a constant offset from one another, tracing a series of approximately parallel curves. This data offers an independent means of determining the error of stabilities and slopes determined by guanidine hydrochloride denaturations and shows that previous error estimates are accurate. More importantly, this behavior cannot be reconciled with a three-state denaturation model for staphylococcal nuclease. The large variations in m_(GuHCl) observed in these mutants must therefore arise from other causes.
机译：在葡萄球菌核酸酶的高度稳定的三重突变体（P117G，H124L和S128A）的背景下进行了六个单取代突变，即V66F，V66G，V66N，V66Q，V66S，V66T和V66Y。野生型葡萄球菌核酸酶，稳定的三重突变体及其六个变异体的热力学稳定性通过盐酸胍在13种不同的pH范围为4.5至10.2的缓冲液中变性来确定。在实验误差范围内，在此宽范围的pH范围内测得的各种蛋白质的DELTAG（H_2o）和m_（GuCl）值相互之间保持恒定的偏移，从而跟踪了一系列近似平行的曲线。该数据提供了一种独立的方法来确定由盐酸胍变性确定的稳定性和斜率的误差，并且表明先前的误差估计是准确的。更重要的是，这种行为无法与葡萄球菌核酸酶的三态变性模型相吻合。因此，在这些突变体中观察到的m_（GuHCl）的巨大变化必须由其他原因引起。

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