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In the unfolding process, it was observed that ovalbumin and ¦Álactalbumin 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 ¦Álactalbumin 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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°®ÓëÓêÏÂ: ½ð±Ò+1 2012-12-21 18:36:03
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