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In the unfolding process, it was observed that ovalbumin and αlactalbumin followed a three state transition pathway involving an intermediate state having high surface hydrophobicity. The intermediate state has also been characterized by circular dichroism spectroscopy, and it was found that the intermediate retained almost the same secondary structure as the native proteins, and therefore it can be referred to as molten globule state. The refolding process was monitored using fluorescence and circular dichroism spectroscopy, and it was observed that the refolding of αlactalbumin was reversible and proceeded through the accumulation of similar type of ntermediates as observed during its unfolding pathway. However, on refolding from the guanidine hydrochloridedenatured state, ovalbumin reached a different folded state. |
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| 在展开过程中观察到，卵清蛋白和乳清蛋白遵循三个状态转变路线包括一个具有强表面疏水性的中间态。中间态用圆二色光谱表征，还发现中间态保留了大多数与天然蛋白质一样的次级结构，因此可以归为熔球态。重折叠过程在荧光和圆二色光谱下观察，也观察到重乳清蛋白折叠过程是可逆的，是在其展开过程中观察到的简单类型中间态的积累。但是，从盐酸胍态的重折叠，卵清蛋白形成一种新的折叠态。 |
2楼2012-12-21 17:28:49
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