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- W4229555667 abstract "The ability of coronaviruses to infect humans is invariably associated with their binding strengths to human receptor proteins. Both SARS-CoV-2, initially named 2019-nCoV, and SARS-CoV were reported to utilize angiotensin-converting enzyme 2 (ACE2) as an entry receptor in human cells. To better understand the interplay between SARS-CoV-2 and ACE2, we performed computational alanine scanning mutagenesis on the “hotspot” residues at protein-protein interfaces using relative free energy calculations. Our data suggest that the mutations in SARS-CoV-2 lead to a greater binding affinity relative to SARS-CoV. In addition, our free energy calculations provide insight into the infectious ability of viruses on a physical basis, and also provide useful information for the design of antiviral drugs." @default.
- W4229555667 created "2022-05-11" @default.
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- W4229555667 date "2020-07-14" @default.
- W4229555667 modified "2023-10-14" @default.
- W4229555667 title "Computational Prediction of Mutational Effects on the SARS-CoV-2 Binding by Relative Free Energy Calculations" @default.
- W4229555667 doi "https://doi.org/10.26434/chemrxiv.11902623.v3" @default.
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