Selected article for: "binding affinity and free energy"

Author: Qiang Huang; Andreas Herrmann
Title: Fast assessment of human receptor-binding capability of 2019 novel coronavirus (2019-nCoV)
  • Document date: 2020_2_3
  • ID: eecyduzq_20
    Snippet: As mentioned, according to statistical thermodynamics, the sampled binding 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 It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the .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 9 obtained in the Monte Carlo docking simulations can be considered to be thermodynamically probable in the binding process of S-protei.....
    Document: As mentioned, according to statistical thermodynamics, the sampled binding 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 It is made available under a The copyright holder for this preprint (which was not peer-reviewed) is the .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 9 obtained in the Monte Carlo docking simulations can be considered to be thermodynamically probable in the binding process of S-protein to ACE2. Indeed, the binding free-energy (or binding affinity) is defined as a thermodynamic average of the binding energies over all possible binding modes of two interacting components. Therefore, the binding free-energy is approximated by the thermodynamic average of the binding energies of all the sampled low-energy conformations as:

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