• Login
    • University Home
    • Library Home
    • Lib Catalogue
    • Advance Search
    View Item 
    •   IR@KDU Home
    • FACULTY STAFF PUBLICATIONS
    • Journal Articles
    • View Item
    •   IR@KDU Home
    • FACULTY STAFF PUBLICATIONS
    • Journal Articles
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Molecular Chaperone ClpB Becomes a Novel Antimicrobial Target

    Thumbnail
    View/Open
    Molecular Chaperone ClpB Becomes a Novel.pdf (386.2Kb)
    Date
    2023-01-01
    Author
    Ranaweera, CB
    Metadata
    Show full item record
    Abstract
    Proteins are the most versatile and complicated biological macromolecules. Protein aggregation is defined as a non-physiological association of misfolded/partially folded polypeptides. Proteostasis prevents or minimizes protein aggregation and keeps proteins soluble and active. In live cells, molecular chaperones and their regulators facilitate protein quality control and proteostasis. A molecular chaperone is a protein that helps other proteins reach their physiologically active native conformation without being present in the client protein's final functional structure. These proteins help de novo protein folding and refolding of misfolded/partially folded proteins under cellular stresses and thereby inhibit protein aggregation.
    URI
    http://ir.kdu.ac.lk/handle/345/6674
    Collections
    • Journal Articles [85]

    Library copyright © 2017  General Sir John Kotelawala Defence University, Sri Lanka
    Contact Us | Send Feedback
     

     

    Browse

    All of IR@KDUCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsFacultyDocument TypeThis CollectionBy Issue DateAuthorsTitlesSubjectsFacultyDocument Type

    My Account

    LoginRegister

    Context

    Edit this item

    Library copyright © 2017  General Sir John Kotelawala Defence University, Sri Lanka
    Contact Us | Send Feedback