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Investigating the effect of different transducer stiffness values on the contactin complex detachment by steered molecular dynamics.
Journal of Molecular Graphics & Modelling 2017 August
This study investigated the adhesion behavior of Contactin4 (CNTN4), a member of Immunoglobulin Super Family (Ig-SF) of cell adhesion molecules. Contactin4 plays a crucial role in the formation, maintenance, and plasticity of neuronal networks. Contactin in its complex configuration with protein tyrosine phosphatase gamma (PTPRG) was selected for simulation. By utilizing Steered Molecular Dynamics (SMD), the uniaxial force was applied to induce unbinding of the complex, and the force-induced detachment of complex components was probed. Three sets of simulations with three values of transducer stiffness and five pulling speeds were designed. Our results showed the dependence of unbinding force on both accessible parameters of pulling speed and spring stiffness. By increasing the stiffness value and pulling speed the rupture force increased. Accordingly, the dissociation rates due to the Bell's theory based on rupture forces and loading rates were calculated.
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