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首页> 外文期刊>Langmuir: The ACS Journal of Surfaces and Colloids >Secondary structural changes of homologous proteins, lysozyme and α-lactalbumin, in thermal denaturation up to 130 ° c and sodium dodecyl sulfate (SDS) effects on these changes: Comparison of thermal stabilities of sds-induced helical structures in these proteins
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Secondary structural changes of homologous proteins, lysozyme and α-lactalbumin, in thermal denaturation up to 130 ° c and sodium dodecyl sulfate (SDS) effects on these changes: Comparison of thermal stabilities of sds-induced helical structures in these proteins

机译：同源蛋白，溶菌酶和α-乳清蛋白的二级结构变化在高达130°c的热变性和十二烷基硫酸钠（SDS）中对这些变化的影响：比较这些蛋白中sds诱导的螺旋结构的热稳定性

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摘要

The thermal stability of two homologous proteins, lysozyme and α-lactalbumin, was examined by circular dichroism. The present study clearly showed two different aspects between the homologous proteins: (1) the original helices of lysozyme and α-lactalbumin were unchanged at heat treatments up to 60 and 40 °C, respectively, indicating a higher thermal stability of lysozyme, and (2) upon cooling to 25 °C, the original helices of lysozyme were never reformed after they were once disrupted, while those of α-lactalbumin, disrupted at a particular temperature range between 40 and 60 °C, were completely reformed. In addition, the structural changes were also examined in the coexistence of sodium dodecyl sulfate (SDS), which induced the formation of helical structures in these proteins at 25 °C. A distinct difference appeared in the thermal stabilities of the SDS-induced helices. All of the SDS-induced helices of lysozyme were disrupted below 60 °C, while those of α-lactalbumin at 10 mM SDS were unchanged up to 130 °C. A similarity was also fixed. Not only the SDS-induced helices but also the original helices of the two proteins were reformed upon cooling to 25 °C after the thermal denaturation below 100 °C in the coexistence of 10 mM SDS.
机译：通过圆二色性检查了两种同源蛋白，溶菌酶和α-乳清蛋白的热稳定性。本研究清楚地表明了同源蛋白之间的两个不同方面：（1）溶菌酶和α-乳清蛋白的原始螺旋分别在高达60和40°C的热处理下没有变化，表明溶菌酶的热稳定性更高;和（ 2）冷却至25°C后，溶菌酶的原始螺旋一旦被破坏，就不会再进行重组，而在40至60°C的特定温度范围内破坏的α-乳清蛋白则完全被重组。此外，还检查了十二烷基硫酸钠（SDS）的共存情况下的结构变化，这在25°C时诱导了这些蛋白质中螺旋结构的形成。 SDS诱导的螺旋的热稳定性出现了明显的差异。在60°C以下，所有SDS诱导的溶菌酶螺旋均被破坏，而在130°C时，在10 mM SDS下α-乳清蛋白的螺旋线未发生变化。相似性也已修复。在10 mM SDS共存下低于100°C进行热变性后，冷却至25°C时，不仅SDS诱导的螺旋而且两种蛋白质的原始螺旋均得以重整。

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