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    <mods:titleInfo>
        <mods:title>Stability and location of mutant proteins in bacterial cells</mods:title>
    </mods:titleInfo>
    <mods:name type="personal">
        <mods:namePart>Spangle, Dylan</mods:namePart>
        <mods:role>
            <mods:roleTerm type="text">creator</mods:roleTerm>
        </mods:role>

    </mods:name>
    <mods:name type="personal">
        <mods:namePart>Weinreich, Daniel</mods:namePart>
        <mods:role>
            <mods:roleTerm type="text">advisor</mods:roleTerm>
        </mods:role>
        <mods:affiliation>Brown University. Department of Ecology and Evolutionary
            Biology</mods:affiliation>
    </mods:name>

    <mods:name type="corporate">
        <mods:namePart>Brown University. Undergraduate Teaching and Research Award</mods:namePart>
        <mods:role>
            <mods:roleTerm type="text">research program</mods:roleTerm>
        </mods:role>

    </mods:name>

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    <mods:genre authority="aat">posters</mods:genre>
    <mods:originInfo>
        <mods:place>
            <mods:placeTerm type="text">Providence</mods:placeTerm>
        </mods:place>
        <mods:publisher>Brown University</mods:publisher>
        <mods:dateCreated encoding="w3cdtf">2015-08-07</mods:dateCreated>
    </mods:originInfo>
    <mods:physicalDescription>
        <mods:extent>1 poster</mods:extent>
        <mods:digitalOrigin>reformatted digital</mods:digitalOrigin>
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    <mods:abstract>Evolution by selection begins at the molecular level within the cell: a series of
        mutations occur that are able to become fixed in the population, and finally lead to a
        protein sequence that performs a novel function for the organism. ß-lactamase, a bacterial
        protein that counteracts ß-lactam antibiotics such as ampicillin, is a significant and
        well-studied protein, making it an excellent model for studying the biochemical pathway of
        protein evolution. It has been hypothesized that the relative fitness of mutant proteins is
        primarily determined by three factors: catalytic activity at the active site, stability of
        overall folding structure, and localization in the cell. We expressed and purified wild-type
        and mutant alleles of the TEM-1 ß-lactamase gene to study stability and localization of this
        protein. All of these mutations were outside the protein's active site, removing catalytic
        activity at the active site as a variable. We isolated proteins from periplasmic,
        cytosol-soluble and insoluble fractions using established biochemical methods. Subsequently
        these protein samples be analyzed using transverse urea gradient gel electrophoresis and
        Western blot to determine stability of these alleles, and using ELISA to quantitatively
        determine localization.</mods:abstract>
    <mods:subject authority="lcsh">
        <mods:topic>Drug resistance in microorganisms</mods:topic>
    </mods:subject>
    <mods:subject authority="lcsh">
        <mods:topic>Beta-lactamases</mods:topic>
    </mods:subject>
    <mods:subject authority="lcsh">
        <mods:topic>Biochemistry</mods:topic>
    </mods:subject>
<mods:identifier xmlns:xlink="http://www.w3.org/1999/xlink" type="doi">10.26300/a40q-2727</mods:identifier></mods:mods>