REDESIGNING THE HYDROPHOBIC CORE OF A 4-HELIX-BUNDLE PROTEIN
REDESIGNING THE HYDROPHOBIC CORE OF A 4-HELIX-BUNDLE PROTEIN
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DOI：
10.1002/pro.5560031114
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发表时间：
1994-11-01
期刊：
影响因子：
8
通讯作者：
REGAN, L
中科院分区：
文献类型：
--
作者：
MUNSON, M;OBRIEN, R;REGAN, L
合理地重新设计的4-螺旋束蛋白Rop的变体进行了描述。新的蛋白质具有简化的、重新包装的疏水核心，并且再现了野生型蛋白质的结构和天然的物理性质。的重新包装的蛋白质已被其特征在于crystallically和它们的平衡和动力学的热和化学的展开特性进行了比较与野生型代表。相对于野生型蛋白质的热变性的重新包装的蛋白质的平衡稳定性增强。与其他小蛋白相比，野生型Rop的化学诱导折叠和解折叠的速率极其缓慢。有趣的是，尽管重新包装的蛋白质比野生型更热稳定，但与野生型相比，它们的化学诱导折叠和解折叠的速率大大增加。也许由于这个原因，它们对化学变性剂的平衡稳定性与野生型相比略有降低。
Rationally redesigned variants of the 4-helix-bundle protein Rop are described. The novel proteins have simplified, repacked, hydrophobic cores and yet reproduce the structure and native-like physical properties of the wildtype protein. The repacked proteins have been characterized thermodynamically and their equilibrium and kinetic thermal and chemical unfolding properties are compared with those of wild-type Rep. The equilibrium stability of the repacked proteins to thermal denaturation is enhanced relative to that of the wild-type protein. The rate of chemically induced folding and unfolding of wild-type Rop is extremely slow when compared with other small proteins. Interestingly, although the repacked proteins are more thermally stable than the wild type, their rates of chemically induced folding and unfolding are greatly increased in comparison to wild type. Perhaps as a consequence of this, their equilibrium stabilities to chemical denaturants are slightly reduced in comparison to the wild type.