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Mapping the allosteric effects that define functional activity of SARS-CoV-2 specific antibodies
[article]
2021
bioRxiv
pre-print
AbstractPrevious studies on the structural relationship between human antibodies and SARS-CoV-2 have focused on generating static snapshots of antibody complexes with the Spike trimer. However, antibody-antigen interactions are dynamic, with significant binding-induced allosteric effects on conformations of antibody and its target antigen. In this study, we employ hydrogen-deuterium exchange mass spectrometry, in vitro assays, and molecular dynamics simulations to investigate the allosteric
doi:10.1101/2021.12.27.474251
fatcat:bzvxjxpm5vfy5ajmuezqta6vwy