Intermediate states in protein folding.
Intermediate states in protein folding.
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蛋白质折叠的中间状态。
DOI：
10.1006/jmbi.1996.0280
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发表时间：
1996
期刊：
影响因子：
--
通讯作者：
Privalov,PL
中科院分区：
文献类型：
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作者：
Privalov,PL
蛋白质折叠的效率表明，这一过程通过一些中间状态进行，提高了实验观察蛋白质不完全折叠状态的可能性。然而，观察到的部分折叠的稳定状态的蛋白质的关键分析表明，它们呈现出错误折叠的形式下获得的折叠不适当的条件下，或部分未折叠的状态，保留折叠的子部分，这些分子。这个保留的部分，展开最后和折叠第一次在展开/重折叠实验中，有一个明确的三级结构保持特定的长程相互作用，并可以通过断裂分离。因此，它可以被认为是蛋白质分子的一个确定的结构域。如果一个小的单结构域蛋白质的多肽链不被错误折叠的形式所困，它的折叠进行得非常迅速，所有的中间体都是短暂的，并且非常不稳定。
The efficiency of protein folding suggests that this process proceeds through some intermediate states, raising the possibility of experimental observation of incompletely folded states of proteins. However, critical analysis of the observed partly folded stable states of proteins shows that they present either misfolded forms obtained under conditions inappropriate for folding, or partially unfolded states that retain folded the subpart of these molecules. This retained part, which unfolds last and folds first in a unfolding/refolding experiment, has a definite tertiary structure maintained by specific long-range interactions and can be isolated by fragmentation. Therefore, it can be regarded as a definite domain of the protein molecule. Provided the polypeptide chain of a small single domain protein does not become trapped in a misfolded form, its folding proceeds very rapidly, with all intermediates being transient and extremely unstable.