Joh Nathan H, Oberai Amit, Yang Duan, Whitelegge Julian P, Bowie James U
Department of Chemistry and Biochemistry, UCLA-DOE Center for Genomics and Proteomics, Molecular Biology Institute, University of California, Los Angeles, California 90095, USA.
J Am Chem Soc. 2009 Aug 12;131(31):10846-7. doi: 10.1021/ja904711k.
A major driving force for water-soluble protein folding is the hydrophobic effect, but membrane proteins cannot make use of this stabilizing contribution in the apolar core of the bilayer. It has been proposed that membrane proteins compensate by packing more efficiently. We therefore investigated packing contributions experimentally by observing the energetic and structural consequences of cavity creating mutations in the core of a membrane protein. We observed little difference in the packing energetics of water and membrane soluble proteins. Our results imply that other mechanisms are employed to stabilize the structure of membrane proteins.
水溶性蛋白质折叠的一个主要驱动力是疏水效应，但膜蛋白无法利用双层膜非极性核心中的这种稳定作用。有人提出膜蛋白通过更高效的堆积来补偿。因此，我们通过观察膜蛋白核心中产生空腔突变的能量和结构后果，对堆积作用进行了实验研究。我们观察到水溶性蛋白和膜溶性蛋白在堆积能量方面几乎没有差异。我们的结果表明，膜蛋白结构的稳定采用了其他机制。
