Ligand binding: Molecular mechanics calculation of the streptavidin biotin rupture force
Ligand binding: Molecular mechanics calculation of the streptavidin biotin rupture force
复制标题
DOI：
10.1126/science.271.5251.997
复制
发表时间：
1996-02-16
期刊：
影响因子：
56.9
通讯作者：
Tavan, P
中科院分区：
文献类型：
--
作者：
Grubmuller, H;Heymann, B;Tavan, P
此处通过计算机模拟计算使链霉亲和素-生物素复合物破裂所需的力。计算得到的力与最近的单分子原子力显微镜实验结果吻合得很好。这些模拟表明了一个详细的多途径断裂机制，涉及五个主要的解除绑定的步骤。结合力和特异性归因于生物素配体与链霉亲和素结合口袋内残基之间的氢键网络。在断裂过程中，额外的水桥大大提高了复合物的稳定性，甚至主导了结合相互作用。与此相反，空间位阻似乎没有贡献的结合力，虽然观察到构象运动。
The force required to rupture the streptavidin-biotin complex was calculated here by computer simulations. The computed force agrees well with that obtained by recent single molecule atomic force microscope experiments. These simulations suggest a detailed multiple-pathway rupture mechanism involving five major unbinding steps. Binding forces and specificity are attributed to a hydrogen bond network between the biotin ligand and residues within the binding pocket of streptavidin. During rupture, additional water bridges substantially enhance the stability of the complex and even dominate the binding interactions. In contrast, steric restraints do not appear to contribute to the binding forces, although conformational motions were observed.