JavaScript is disabled for your browser. Some features of this site may not work without it.
  • About K
  • Academics
  • Admission
  • Alumni Relations
  • Giving to K
  • News & Events
  • Student Life
  • HORNET HIVE
  • ATHLETICS
  • SITEMAP
  • WEBMAIL
    • Login
    View Item 
    •   CACHE Homepage
    • Academic Departments, Programs, and SIPs
    • Physics
    • Physics Senior Integrated Projects
    • View Item
    •   CACHE Homepage
    • Academic Departments, Programs, and SIPs
    • Physics
    • Physics Senior Integrated Projects
    • View Item

    Using Point Arrays to Characterize Drug-Bound Hepatitis B Virus and Human Enterovirus 71 Capsid Structures

    Thumbnail
    View/Open
    Searchable PDF/Kalamazoo College Only (48.02Mb)
    Date
    2021-11-01
    Author
    Rogowski, Lily
    Metadata
    Show full item record
    Abstract
    A virus capsid is composed of identical protein subunits which occupy chemically equivalent environments and assemble according to icosahedral symmetry. This protein shell holds critical roles throughout the viral life cycle including protecting the viral genome, facilitating binding to a host, and initiating viral replication. Because the capsid ultimately allows for infection, disrupting its symmetry has been identified as a promising strategy for antiviral treatments. This study focused on using point arrays to characterize the structural changes of drug-bound Hepatitis B Virus (HBV) and Human Enterovirus 71 (HEV-71) capsids. Point arrays represent the geometric constraints that icosahedral viruses conform to and provide insight into key protein associations and sites of stability at multiple radial levels. In this study, small molecule drugs intended to disrupt the capsid structure of HBV and compounds aimed to stabilize the structure of HEV-71 were analyzed. The results demonstrated that drug binding leads to a greater number of point array fits for the drugbound structures. The broad range of fits were consistent with the gauge point used to characterize the native capsids, yet also introduced new gauge point fits. These observations suggest that binding increases the conformational flexibility of the capsid as well as its stability. Additionally, the multiple fits proposed new locations of interest which may contribute to enhancing the stability of the capsid structure. Overall, point arrays were successfully fit to drug-bound virus capsids and these results demonstrate that point arrays are a valuable tool for assessing conformational changes caused by binding.
    URI
    https://cache.kzoo.edu/handle/10920/43752
    Collections
    • Physics Senior Integrated Projects [329]

    Browse

    All of DSpaceCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    Login

    DSpace software copyright © 2002-2023  DuraSpace
    DSpace Express is a service operated by 
    Atmire NV
    Logo

    Kalamazoo College
    1200 Academy Street
    Kalamazoo Michigan 49006-3295
    USA
    Info 269-337-7000
    Admission 1-800-253-3602

    About K
    Academics
    Admission
    Alumni Relations
    Giving to K
    News & Events
    Student Life
    Sitemap
    Map & Directions
    Contacts
    Directories
    Nondiscrimination Policy
    Consumer Information
    Official disclaimer
    Search this site


    Academic Calendars
    Apply
    Bookstore
    Crisis Response
    Employment
    Library
    Registrar
    DSpace Express is a service operated by 
    Atmire NV