Glycosylation is a post-translational modification of proteins in which carbohydrate chains, known asglycans, are linked to lipids or proteins. Many biological proteins are glycosylated, and these glycans are important in the necessary biological functionality of proteins. In this dissertation, the structure/function relationship of highly glycosylated proteins are explored using molecular dynamics simulations and experiment in concert, specifically: 1) the structural & mechanistic explanation of preventing COVID-19 infection with a novel inhaled antiviral compound, 2) the dynamics of the SARS-CoV-2 spike glycoprotein interacting with its cofactors on the host-cell and exploitation of said interaction to develop a rapid antigen test, 3) the mechanism of airborne transmission of the SARS-CoV-2 virion in a respiratory aerosol, and 4) the relationship between glycosylation and functional dynamics of T-cell immunoglobulin and mucin domain containing proteins.
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