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SARS-COV-2 envelope protein induces membrane curvature through asymmetric hydrophobic mismatch
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Sandberg, Jesse. SARS-COV-2 envelope protein induces membrane curvature through asymmetric hydrophobic mismatch. Retrieved from https://doi.org/doi:10.7282/t3-xdb1-1p17

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TitleSARS-COV-2 envelope protein induces membrane curvature through asymmetric hydrophobic mismatch
NameSandberg, Jesse (author); Brannigan, Grace (chair); Klein, Eric (member); Lamoureux, Guillaume (member); Rutgers University; Graduate School - Camden
Date Created2021
Other Date2021-10 (degree)
SubjectBiophysics, Computational physics
Extent1 online resource (v, 41 pages)
DescriptionThe SARS-CoV-2 Envelope (E) protein is an integral membrane protein and is implicated in numerous viral processes including but not limited to assembly, budding, envelope formation, and pathogenesis. While much work has recently been done to characterize this protein's structure, function, and interactions with other proteins, its interactions with and effects on surrounding membranes are less well understood. E is known to express in the Endoplasmic Reticulum Golgi Intermediate Complex (ERGIC) where it aids in the budding process by inducing curvature on the ERGIC membrane, helping push a new virion outward. When E is mutated in a related virus, the virus loses its characteristic spherical shape and becomes less capable of infecting new cells. This suggests that better understanding of E's ability to induce membrane curvature in SARS-CoV-2 may be useful in the fight against COVID-19. Using Coarse Grain Molecular Dynamics (CG-MD) simulations and an elastic simulation of our own design, we computationally studied the bending effect of the E protein in a variety of model membranes. Our results strongly suggest that E's bending mechanism is driven by the combination of E's asymmetric shape and the degree of hydrophobic mismatch between E and the surrounding membrane.
NoteM.S.
NoteIncludes bibliographical references
Genretheses
Persistent URLhttps://doi.org/doi:10.7282/t3-xdb1-1p17
LanguageEnglish
CollectionCamden Graduate School Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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