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• W3181568045 abstract "Abstract Highly detailed steered Molecular Dynamics simulations are performed on differently glycosylated receptor binding domains of the SARS-CoV-2 spike protein. The binding strength and the binding range increases with glycosylation. The interaction energy rises very quickly with pulling the proteins apart and only slowly drops at larger distances. We see a catch slip type behavior where interactions during pulling break and are taken over by new interactions forming. The dominant interaction mode are hydrogen bonds but Lennard-Jones and electrostatic interactions are relevant as well. Statement of Significance Glycosylation of the receptor binding domain of the Spike protein of SARS-CoV-2 as well as the ACE2 receptor leads to stronger and longer ranged binding interactions between the proteins. Particularly, at shorter distances the interactions are between residues of the proteins themselves whereas at larger distances these interactions are mediated by the glycans. Abstract Figure" @default.
• W3181568045 created "2021-07-19" @default.
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• W3181568045 date "2021-07-15" @default.
• W3181568045 modified "2023-10-16" @default.
• W3181568045 title "SARS-Cov-2 Spike binding to ACE2 is stronger and longer ranged due to glycan interaction" @default.
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• W3181568045 doi "https://doi.org/10.1101/2021.07.15.452507" @default.
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