Unbinding of the Streptavidin-biotin Complex by Atomic Force Microscopy: A Hybrid Simulation Study
Resource
The Journal of Chemical Physics 125: 104905
Journal
The Journal of Chemical Physics
Journal Issue
104905
Pages
-
Date Issued
2006
Date
2006
Author(s)
Abstract
A hybrid molecular simulation technique, which combines molecular dynamics and continuum mechanics, was used to study the single-molecule unbinding force of a streptavidin-biotin complex. The hybrid method enables atomistic simulations of unbinding events at the millisecond time scale of atomic force microscopy (AFM) experiments. The logarithmic relationship between the unbinding force of the streptavidin-biotin complex and the loading rate (the product of cantilever spring constant and pulling velocity) in AFM experiments was confirmed by hybrid simulations. The unbinding forces, cantilever and tip positions, locations of energy barriers, and unbinding pathway were analyzed. Hybrid simulation results from this work not only interpret unbinding AFM experiments but also provide detailed molecular information not available in AFM experiments. © 2006 American Institute of Physics.
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journal article
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