Cieplak Marek, Hoang Trinh Xuan, Robbins Mark O
Department of Physics and Astronomy, The Johns Hopkins University, Baltimore, Maryland 21218, USA.
Phys Rev E Stat Nonlin Soft Matter Phys. 2004 Jan;69(1 Pt 1):011912. doi: 10.1103/PhysRevE.69.011912. Epub 2004 Jan 30.
Mechanical stretching of six proteins is studied through molecular dynamics simulations. The model is Go-like, with Lennard-Jones interactions at native contacts. Low-temperature unfolding scenarios are remarkably complex and sensitive to small structural changes. Thermal fluctuations reduce the peak forces and the number of metastable states during unfolding. The unfolding pathways also simplify as temperature rises. In the entropic limit, all proteins show a monotonic decrease of the extension where bonds rupture with their separation along the backbone (contact order).
通过分子动力学模拟研究了六种蛋白质的机械拉伸。该模型类似于戈模型，在天然接触处存在 Lennard-Jones 相互作用。低温下的解折叠情况非常复杂，并且对小的结构变化很敏感。热涨落会降低解折叠过程中的峰值力和亚稳态的数量。随着温度升高，解折叠途径也会简化。在熵极限下，所有蛋白质沿主链（接触序）的键断裂时，其伸长都会单调下降。
