Favrin Giorgio, Irbäck Anders, Wallin Stefan
Complex Systems Division, Department of Theoretical Physics, Lund University, Lund, Sweden.
Proteins. 2004 Jan 1;54(1):8-12. doi: 10.1002/prot.10575.
Z(SPA-1) is an engineered protein that binds to its parent, the three-helix-bundle Z domain of staphylococcal protein A. Uncomplexed Z(SPA-1) shows a reduced helix content and a melting behavior that is less cooperative, compared with the wild-type Z domain. Here we show that the difference in folding behavior between these two sequences can be partly understood in terms of an off-lattice model with 5-6 atoms per amino acid and a minimalistic potential, in which folding is driven by backbone hydrogen bonding and effective hydrophobic attraction.
Z(SPA-1)是一种经过工程改造的蛋白质，它能与其母体——葡萄球菌蛋白A的三螺旋束Z结构域相结合。与野生型Z结构域相比，未复合的Z(SPA-1)呈现出较低的螺旋含量以及不太协同的解链行为。在此我们表明，这两个序列在折叠行为上的差异，部分可以通过一个每个氨基酸有5至6个原子且具有简约势的非晶格模型来理解，在该模型中，折叠由主链氢键和有效的疏水吸引力驱动。
