链霉亲和素
位阻效应
配体(生物化学)
生物素
化学
分子动力学
氢键
分子
结合位点
生物物理学
化学物理
原子力显微镜
结晶学
纳米技术
材料科学
计算化学
立体化学
生物化学
受体
生物
有机化学
作者
Helmut Grubmüller,Berthold Heymann,Paul Tavan
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:1996-02-16
卷期号:271 (5251): 997-999
被引量:863
标识
DOI:10.1126/science.271.5251.997
摘要
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.
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