ALTERNATIVE PACKING ARRANGEMENTS IN THE HYDROPHOBIC CORE OF LAMBDA-REPRESSOR
ALTERNATIVE PACKING ARRANGEMENTS IN THE HYDROPHOBIC CORE OF LAMBDA-REPRESSOR
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DOI：
10.1038/339031a0
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发表时间：
1989-05-04
期刊：
影响因子：
64.8
通讯作者：
SAUER, RT
中科院分区：
文献类型：
--
作者：
LIM, WA;SAUER, RT
λ 阻遏物 N 端结构域中疏水核心位置的随机改变（无论是单独还是组合）表明，重新包装蛋白质核心的方法有很多种。尽管功能序列的数量受到组成、体积和空间相互作用的限制，但这些位置保持疏水性的简单要求是核心序列是否与野生型折叠相容的主要决定因素。
The random alteration of hydrophobic core positions in the N-terminal domain of λ-repressor, both individually and in combination, shows that there are many ways of repacking the core of the protein. Although the number of functional sequences is limited by constraints on composition, volume and steric interactions, the simple requirement that these positions remain hydrophobic is the main determinant of whether a core sequence is compatible with the wild-type fold.