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E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies
Wei Bu Wang, Yu Liang, Yu Qin Jin, Jing Zhang, View ORCID ProfileJi Guo Su, Qi Ming Li
doi: https://doi.org/10.1101/2021.02.17.431566
Wei Bu Wang
1Key Laboratory for Microstructural Material Physics of Hebei Province, School of Science, Yanshan University, Qinhuangdao 066004, China
Yu Liang
2The Sixth Laboratory, National Vaccine and Serum Institute, Beijing 101111, China
Yu Qin Jin
2The Sixth Laboratory, National Vaccine and Serum Institute, Beijing 101111, China
Jing Zhang
2The Sixth Laboratory, National Vaccine and Serum Institute, Beijing 101111, China
Ji Guo Su
1Key Laboratory for Microstructural Material Physics of Hebei Province, School of Science, Yanshan University, Qinhuangdao 066004, China
2The Sixth Laboratory, National Vaccine and Serum Institute, Beijing 101111, China
Qi Ming Li
2The Sixth Laboratory, National Vaccine and Serum Institute, Beijing 101111, China
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Posted February 17, 2021.
E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies
Wei Bu Wang, Yu Liang, Yu Qin Jin, Jing Zhang, Ji Guo Su, Qi Ming Li
bioRxiv 2021.02.17.431566; doi: https://doi.org/10.1101/2021.02.17.431566
E484K mutation in SARS-CoV-2 RBD enhances binding affinity with hACE2 but reduces interactions with neutralizing antibodies and nanobodies: Binding free energy calculation studies
Wei Bu Wang, Yu Liang, Yu Qin Jin, Jing Zhang, Ji Guo Su, Qi Ming Li
bioRxiv 2021.02.17.431566; doi: https://doi.org/10.1101/2021.02.17.431566
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