• Login
    View Item 
    •   Shocker Open Access Repository Home
    • Graduate Student Research
    • ETD: Electronic Theses and Dissertations
    • Dissertations
    • View Item
    •   Shocker Open Access Repository Home
    • Graduate Student Research
    • ETD: Electronic Theses and Dissertations
    • Dissertations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Single molecule biophysics and fluorescence correlation spectroscopy

    View/Open
    d14040_Wang.pdf (2.607Mb)
    Date
    2014-12
    Author
    Wang, Zifan
    Advisor
    English, Douglas S.
    Metadata
    Show full item record
    Abstract
    This dissertation focuses on applications of ultra-sensitive fluorescence. It mainly contains two parts: applying single molecule Foerster resonance energy transfer (SM-FRET) in studies of dynamics and topology of looping constructs formed from DNA-protein interaction and developing a novel fluorescence correlation spectroscopy (FCS) approach to measure binding between drug molecules and different vesicles. Foerster resonance energy transfer (FRET) is a distance dependent phenomenon that can be used to detect and quantify biochemical conformations and interactions in complex samples. With ensemble measurements, it is impossible to resolve the information for dynamic heterogeneous systems without averaging the result. SM-FRET, achieved by using confocal microscopy, measures the signal from a single molecule at a time, thus eliminates ensemble averaging. In this case, SM-FRET was used to evaluate conformational dynamics in a model of negative gene regulation. Details will be discussed in chapter 1, 3 and 4. In FCS measurements, the fluctuations of fluorescence intensity of the sample is correlated to determine information from the processes that cause the fluctuations such as molecules diffusing in and out of a laser focal observation volume and intersystem crossing. In this dissertation, intensity fluctuations caused by intersystem crossing and diffusion are utilized to develop a new FCS approach. This FCS approach can further be used to determine the binding of fluorophores to larger structures. Details will be discussed in chapter 2, 5, 6 and 7.
    Description
    Thesis (Ph.D.)-- Wichita State University, Fairmount College of Liberal Arts and Sciences, Dept. of Chemistry
    URI
    http://hdl.handle.net/10057/11372
    Collections
    • CHEM Theses and Dissertations
    • Dissertations
    • LAS Theses and Dissertations

    Browse

    All of Shocker Open Access RepositoryCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsBy TypeThis CollectionBy Issue DateAuthorsTitlesSubjectsBy Type

    My Account

    LoginRegister

    Statistics

    Most Popular ItemsStatistics by CountryMost Popular Authors

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