• Login
    View Item 
    •   Carroll Scholars Home
    • Life and Environmental Sciences
    • Life and Environmental Sciences Undergraduate Theses
    • View Item
    •   Carroll Scholars Home
    • Life and Environmental Sciences
    • Life and Environmental Sciences Undergraduate Theses
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Toward Solving the Structure of Cholesterol Oxidase H447E/E361Q Double Mutant

    Thumbnail
    View/Open
    2004_KrauseL_THS_000790.pdf (1.747Mb)
    Author
    Krause, Larryn
    Advisor
    Ron Wilde; Marilyn Schendel; Sam Alvey
    Date of Issue
    2004-04-01
    Metadata
    Show full item record
    URI
    https://scholars.carroll.edu/handle/20.500.12647/2961
    Title
    Toward Solving the Structure of Cholesterol Oxidase H447E/E361Q Double Mutant
    Type
    thesis
    Abstract
    Cholesterol oxidase, a bifunctional flavoenzyme facilitates the oxidation and isomerization of cholesterol. Wild type cholesterol oxidase has been crystallized, and its structure has been resolved to 0.95 A. Wild type cholesterol oxidase turns over cholesterol with such extreme efficiency that it is very difficult to crystallize the substrate-enzyme complex. Cholesterol oxidase H447E/E361Q double mutant, which binds cholesterol, but is unable to completely turn it over, was expressed, purified, and crystallized to obtain a crystal structure. Once solved, the structure of the cholesterol oxidase double mutant could then be used as a background structure for the crystallization of the substrate-enzyme complex. Cholesterol oxidase H447E/E361Q double mutant, which binds cholesterol, but is unable to completely turn it over, was expressed, purified, and crystallized to obtain a crystal structure. Once solved, the structure of the cholesterol oxidase double mutant could then be used as a background structure for the crystallization of the substrate-enzyme complex. In an attempt to obtain a control for future experimentation on the substrate-enzyme complex, x-ray crystallographic methods were utilized. These methods yielded high-resolution data to 1.5 A.
    Degree Awarded
    Bachelor's
    Semester
    Spring
    Department
    Life & Environmental Sciences
    Collections
    • Life and Environmental Sciences Undergraduate Theses

    Browse

    All of Carroll ScholarsCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

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