CONTRIBUTION OF HYDROPHOBIC INTERACTIONS TO PROTEIN STABILITY
CONTRIBUTION OF HYDROPHOBIC INTERACTIONS TO PROTEIN STABILITY
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DOI：
10.1038/333784a0
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发表时间：
1988-06-23
期刊：
影响因子：
64.8
通讯作者：
FERSHT, AR
中科院分区：
文献类型：
--
作者：
KELLIS, JT;NYBERG, K;FERSHT, AR
蛋白质折叠的一个主要因素是疏水侧链的掩埋。一个具体的例子是通过非极性侧链的交错将α-螺旋堆积在β-折叠上。这些相互作用对蛋白质稳定性能量学的贡献可以通过简单的蛋白质工程实验来测量。我们已经使用定点诱变来截短来自解淀粉芽孢杆菌的小核糖核酸酶（芽孢杆菌RNA酶）中α-螺旋/β-折叠界面处的疏水侧链。突变蛋白稳定性的降低通过它们对尿素变性的敏感性来测量。形成一个-CH 2-基团大小的空穴会使酶不稳定1.1 kcal mol−1，而形成三个这样的基团大小的空穴会使酶不稳定4.0 kcal mol−1。
A major factor in the folding of proteins is the burying of hydro-phobic side chains. A specific example is the packing ofα-helices onβ-sheets by interdigitation of nonpolar side chains. The contri-butions of these interactions to the energetics of protein stability may be measured by simple protein engineering experiments. We have used site-directed mutagenesis to truncate hydrophobic side chains at anα-helix/β-sheet interface in the small ribonuclease fromBacillus amyloliquefadens(barnase). The decreases in stabil-ity of the mutant proteins were measured by their susceptibility to urea denaturation. Creation of a cavity the size of a –CH2–group destabilizes the enzyme by 1.1 kcal mol−1, and a cavity the size of three such groups by 4.0 kcal mol−1.