 We present here a new method to interrogate affinity differences resulting from mutations in a host-virus protein--protein interface. Our method is based on extensive non-equilibrium all-atom simulations: We computationally pull the machupo virus (MACV) spike glycoprotein (GP1) away from the human transferrin receptor (hTfR1) and estimate affinity using the maximum applied force during a pulling simulation and the area under the force-versus-distance curve.
<clarity>  We present here a new method to interrogate affinity differences resulting from mutations in a host-virus protein--protein interface. Our method is based on extensive non-equilibrium all-atom simulations: We computationally pull the machupo virus (MACV) spike glycoprotein (GP1) away from the human transferrin receptor (hTfR1) and estimate affinity using the maximum applied force during a pulling simulation and the area under the force-versus-distance curve.
 We present here a new method to interrogate affinity differences resulting from mutations in a host-virus protein-protein interface. We use steered molecular dynamics (SMD) to computationally pull the machupo virus (MACV) spike glycoprotein (GP1) away from the human transferrin receptor (hTfR1) and estimate affinity using the maximum applied force during a pulling simulation and the area under the force-versus-distance curve.