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Filtering by: Funding statement Supported in part by NIH award R01GM96685 through the NSF/NIH Ecology and Evolution of Infectious Disease Program. Remove constraint Funding statement: Supported in part by NIH award R01GM96685 through the NSF/NIH Ecology and Evolution of Infectious Disease Program. Academic Affiliation Biochemistry and Biophysics Remove constraint Academic Affiliation: Biochemistry and Biophysics

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  • Viral Targeting of Host Hubs: Interactions between the Rabies Virus and LC8

    Creator:
    Jespersen, Nathan E.
    Abstract:
    As obligate intracellular parasites, viruses rely on host machinery for their own reproduction. Viruses are therefore required to interact with a wide variety of host proteins, despite limitations in viral genome size. The most parsimonious method of success is to hijack central and essential proteins, known as hub proteins. LC8...
    Resource Type:
    Dissertation
    Full Text:
    . Jespersen for the degree of Doctor of Philosophy in Biochemistry and Biophysics presented on September 10

  • Context matters : assembly and disorder in the regulation of multivalent complexes

    Creator:
    Jara, Kayla A.
    Abstract:
    Intrinsically disordered proteins (IDPs), protein regions (IDRs), and protein complexes continue to emerge at the forefront of protein science. Proteins and protein regions lacking specific structure are found in all organisms, and often have vital roles in numerous biological processes. Breaking the well-known structure-function paradigm, the understanding of disorder-based functionality...
    Resource Type:
    Dissertation
    Full Text:
    . Jara for the degree of Doctor of Philosophy in Biochemistry and Biophysics presented on May 31, 2022

  • Structural Insights into Novel Sugar Phosphate Cyclases and Flavoenzymes

    Creator:
    Kean, Kelsey M.
    Abstract:
    The function of a protein is defined by its three-dimensional structure, and in understanding the three-dimensional structure of a protein, we gain an understanding of its function and mechanism. Protein structures, especially at high resolution, can provide detailed insights into many elements of enzyme function and catalysis – identifying residues...
    Resource Type:
    Dissertation
    Full Text:
    a broader context for the roles, evolution, and prevalence of these enzymes in nature. Based on

  • Model systems for structural investigations into peroxiredoxin catalysis, conformation change, and inactivation

    Creator:
    Perkins, Arden
    Abstract:
    Peroxiredoxin (Prx) enzymes catalyze the reduction of hydrogen peroxide, peroxynitrous acid, and organic peroxides, and are extremely efficient peroxidases, with k[subscript cat]/K[subscript M] on the order of 10⁷ - 10⁸ M⁻¹ s⁻¹. Besides their role in oxidative stress defense, evidence has accumulated that some eukaryotes, including humans, use Prxs as...
    Resource Type:
    Dissertation
    Full Text:
    to human health is underscored by the occurrence of cancer in some Prx knockout mice; the