Importance of translational entropy of water in biological self-assembly processes like protein folding.

Importance of translational entropy of water in biological self-assembly processes like protein folding.
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DOI:
10.3390/ijms10031064
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发表时间:
2009-03
影响因子:
5.6
通讯作者:
Kinoshita M
Kinoshita M
中科院分区:
生物学2区
文献类型:
--
作者:
Kinoshita M

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我们简要回顾了我们对蛋白质折叠/去折叠机制的研究。在蛋白质折叠等生物自组装过程中,系统中水的可接近平移构型的数量大大增加,导致水熵的大幅增加。通常的观点,只看在蛋白质表面附近的水是能够阐明的大熵增益后,质外体蓝蛋白折叠,这是最近发现在一个新的实验研究,也没有压力和冷变性。随着水的平移熵的强调,我们目前正在构建一个可靠的方法来预测天然结构的蛋白质从它的氨基酸序列。
We briefly review our studies on the folding/unfolding mechanisms of proteins. In biological self-assembly processes such as protein folding, the number of accessible translational configurations of water in the system increases greatly, leading to a large gain in the water entropy. The usual view looking at only the water in the close vicinity of the protein surface is capable of elucidating neither the large entropic gain upon apoplastocyanin folding, which has recently been found in a novel experimental study, nor the pressure and cold denaturation. With the emphasis on the translational entropy of water, we are presently constructing a reliable method for predicting the native structure of a protein from its amino-acid sequence.
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