Imparato A, Pelizzola A, Zamparo M
Dipartimento di Fisica and CNISM, Politecnico di Torino, c. Duca degli Abruzzi 24, Torino, Italy and INFN, Sezione di Torino, Torino, Italy.
Phys Rev Lett. 2007 Apr 6;98(14):148102. doi: 10.1103/PhysRevLett.98.148102.
The mechanical unfolding of proteins is studied by extending the Wako-Saitô-Muñoz-Eaton model. This model is generalized by including an external force, and its thermodynamics turns out to be exactly solvable. We consider two molecules, the 27th immunoglobulin domain of titin and protein PIN1. We determine equilibrium force-extension curves for the titin and study the mechanical unfolding of this molecule, finding good agreement with experiments. By using an extended form of the Jarzynski equality, we compute the free energy landscape of the PIN1 as a function of the molecule length.
通过扩展和佐-斋藤-穆尼奥斯-伊顿模型来研究蛋白质的机械展开。该模型通过引入外力进行了推广,其热力学结果被证明是完全可解的。我们考虑两个分子,肌联蛋白的第27个免疫球蛋白结构域和蛋白质PIN1。我们确定了肌联蛋白的平衡力-伸长曲线,并研究了该分子的机械展开,发现与实验结果吻合良好。通过使用扩展形式的雅尔津斯基等式,我们计算了PIN1的自由能景观作为分子长度的函数。