• Login
    View Item 
    •   UMB Digital Archive
    • School, Graduate
    • Theses and Dissertations All Schools
    • View Item
    •   UMB Digital Archive
    • School, Graduate
    • Theses and Dissertations All Schools
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Browse

    All of UMB Digital ArchiveCommunitiesPublication DateAuthorsTitlesSubjectsThis CollectionPublication DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    Statistics

    Display statistics

    Investigation of the solution structure of a zinc finger peptide with time-resolved fluorescence spectroscopy

    • CSV
    • RefMan
    • EndNote
    • BibTex
    • RefWorks
    Find Full text
    Author
    Eis, Peggy S.
    Advisor
    Lakowicz, Joseph R.
    Date
    1992
    Type
    dissertation
    
    Metadata
    Show full item record
    Abstract
    Zinc finger proteins are a class of nucleic acid binding proteins that tetrahedrally coordinate zinc ion via cysteine (C) and histidine (H) sidechain atoms to form a defined structure. A solution stucture of the CCHH type zinc finger has been determined with 2D NMR and an X-ray crystallographic structure of a zinc finger protein-DNA complex has been solved. However, neither of these methods reveal information about the conformational heterogeneity that exists in a zinc finger domain. Therefore, the solution structure of a single zinc finger peptide of the CCHH type was investigated with fluorescence spectroscopy in the absence and presence of metal ion and in a denatured state. Energy transfer distance distribution measurements were performed on two different donor-acceptor labeled peptides to determine the range of intramolecular distances and the degree of conformational heterogeneity that exists for the peptide in the metal-free and metal-bound state. Anisotropy measurements were also performed to assess the structure of the zinc finger peptide. A single tryptophan, located at the midpoint of the peptide sequence, serves as the energy donor for two different acceptors. One peptide contains a DNS acceptor attached at its amino terminus and another peptide contains a coumarin derivative attached at the {dollar}\epsilon{dollar}-amino group of its carboxy-terminal lysine. The donor-acceptor distance distributions determined for these two peptides in both cases indicated a shorter distance and a unique conformation (narrow distribution) when metal was bound, and a longer distance with greater conformational flexibility when metal ion was absent. Clearly the metal-bound conformation represents a unique, well-defined structure. Comparison of distance distributions measured for metal-free and denatured peptide indicates that there is some residual structure present in the metal-free peptide.
    Description
    University of Maryland, Baltimore. Biochemistry and Molecular Biology. Ph.D. 1992
    Keyword
    Chemistry, Biochemistry
    Biophysics, General
    Identifier to cite or link to this item
    http://hdl.handle.net/10713/2532
    Collections
    Theses and Dissertations All Schools
    Theses and Dissertations School of Medicine

    entitlement

     
    DSpace software (copyright © 2002 - 2023)  DuraSpace
    Quick Guide | Policies | Contact Us | UMB Health Sciences & Human Services Library
    Open Repository is a service operated by 
    Atmire NV
     

    Export search results

    The export option will allow you to export the current search results of the entered query to a file. Different formats are available for download. To export the items, click on the button corresponding with the preferred download format.

    By default, clicking on the export buttons will result in a download of the allowed maximum amount of items.

    To select a subset of the search results, click "Selective Export" button and make a selection of the items you want to export. The amount of items that can be exported at once is similarly restricted as the full export.

    After making a selection, click one of the export format buttons. The amount of items that will be exported is indicated in the bubble next to export format.