Bruscolini Pierpaolo, Pelizzola Alessandro, Zamparo Marco
Instituto BIFI, Universidad de Zaragoza, Calle Corona de Aragón 42, 50009 Zaragoza, Spain.
J Chem Phys. 2007 Jun 7;126(21):215103. doi: 10.1063/1.2738473.
The authors address the problem of downhill protein folding in the framework of a simple statistical mechanical model, which allows an exact solution for the equilibrium and a semianalytical treatment of the kinetics. Focusing on protein 1BBL, a candidate for downhill folding behavior, and comparing it to the WW domain of protein PIN1, a two-state folder of comparable size, the authors show that there are qualitative differences in both the equilibrium and kinetic properties of the two molecules. However, the barrierless scenario which would be expected if 1BBL were a true downhill folder is observed only at low enough temperature.
作者在一个简单的统计力学模型框架内探讨了蛋白质向下折叠的问题，该模型允许对平衡进行精确求解并对动力学进行半解析处理。作者聚焦于具有向下折叠行为候选特征的蛋白质1BBL，并将其与大小相当的双态折叠蛋白PIN1的WW结构域进行比较，结果表明这两种分子在平衡和动力学性质上存在质的差异。然而，只有在足够低的温度下才会观察到如果1BBL是真正的向下折叠蛋白所预期的无障碍情形。
