Stabilizing and destabilizing effects of phenylalanine→F5-phenylalanine mutations on the folding of a small protein
Stabilizing and destabilizing effects of phenylalanine→F5-phenylalanine mutations on the folding of a small protein
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DOI：
10.1021/ja0634573
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发表时间：
2006-12-20
影响因子：
15
通讯作者：
Gellman, Samuel H.
中科院分区：
文献类型：
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作者：
Woll, Matthew G.;Hadley, Erik B.;Gellman, Samuel H.
我们对鸡绒毛头亚域（c-VHP）的35个残基苯丙氨酸-五氟苯丙氨酸（Phe→F5-Phe）突变体进行了系统评估，其疏水核心具有三个Phe侧链（残基6、10和17）。Phe→F5-Phe突变是有趣的，因为最佳几何形状的芳基-全氟芳基相互作用本质上比芳基-芳基相互作用更有利，因为全氟芳基单位比类似的芳基单位更疏水。一个突变体，phe10→F5-Phe，相对于原生序列提供了增强的三级结构稳定性。分析的其他六个突变体导致稳定性下降。
We report a systematic evaluation of phenylalanine-to-pentafluorophenylalanine (Phe → F5-Phe) mutants for the 35-residue chicken villin headpiece subdomain (c-VHP), the hydrophobic core of which features a cluster of three Phe side chains (residues 6, 10, and 17). Phe → F5-Phe mutations are interesting because aryl−perfluoroaryl interactions of optimal geometry are intrinsically more favorable than aryl−aryl interactions and because perfluoroaryl units are more hydrophobic than are analogous aryl units. One mutant, Phe-10 → F5-Phe, provides enhanced tertiary structural stability relative to the native sequence. The other six mutants analyzed caused a decrease in stability.