Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins
Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins
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DOI：
10.2174/0929866043478220
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发表时间：
2004-04-01
影响因子：
1.6
通讯作者：
Tokunaga, M
中科院分区：
文献类型：
--
作者：
Arakawa, T;Tokunaga, M
一般来说，嗜盐蛋白质仅在高浓度盐的存在下才稳定。高盐浓度不仅对嗜盐蛋白的结构稳定性很重要，而且变性嗜盐蛋白的重折叠也需要高盐浓度。本文综述了静电屏蔽和疏水相互作用在嗜盐蛋白稳定性和重折叠中的重要性。
In general, halophilic proteins are stable only in the presence of salts at high concentrations. Not only is high salt concentration important for structural stability of halophilic proteins, but also refolding of a denatured halophilic protein requires high salt concentration. This review summarizes the importance of electrostatic charge shielding and hydrophobic interactions in the stability and refolding of halophilic proteins.