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- W4254457008 abstract "Understanding thermodynamics and kinetics of the binding process of antibody to SARS-CoV-2 receptor-binding domain (RBD) of Spike protein is very important for the development of COVID19 vaccines. Especially, it is essential to understand how the binding mechanism may change under the effects of RBD mutations. In this context, we have demonstrated that the South African variant (B1.351 or 501Y.V2) can resist the neutralizing antibody (NAb). Three substitutions in RBD including K417N, E484K, and N501Y alters the free energy landscape, binding pose, binding free energy, binding kinetics, and unbinding pathway of RBD + NAb complexes. The low binding affinity of NAb to 501Y.V2 RBD confirms the antibody resistance of the South African variant." @default.
- W4254457008 created "2022-05-12" @default.
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- W4254457008 date "2021-04-07" @default.
- W4254457008 modified "2023-10-11" @default.
- W4254457008 title "Thermodynamics and Kinetics in Antibody Resistance of the 501Y.V2 SARS-CoV-2 Variant" @default.
- W4254457008 doi "https://doi.org/10.26434/chemrxiv.14377361.v1" @default.
- W4254457008 hasPublicationYear "2021" @default.
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