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Abstract:
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.
