Fast assessment of human receptor-binding capability of 2019 novel coronavirus (2019-nCoV)

Qiang Huang; Andreas Herrmann

Using this approach, we sampled a large number of low-energy conformations of S-RBD in complex with ACE2 by preforming multiple, independent docking runs (i.e., simulations), and calculated their binding energies with a physically realistic, all-atom energy function for macromolecular modeling and design (Alford et al., 2017) . According to statistical thermodynamics, the sampled conformations . CC-BY-NC-ND 4.0 International license author/funder. It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.02.01.930537 doi: bioRxiv preprint are considered to be accessible in the real-world process of S-protein binding to ACE2, depending on their thermodynamic probabilities determined by the binding energies.