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Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1

Abstract Details

2003, Bachelor of Science, Miami University, College of Arts and Sciences - Chemistry.
The metallo-b-lactamase L1 has interesting fluorescence properties due to one or more of its five tryptophan residues. In order to determine which tryptophan residues were responsible for fluorescence quenching upon substrate binding and fluorescence plateauing due to preferential Zn(II) binding in the active site, substitutions of asparagine were made for each tryptophan. Four of the five mutants produced only insoluble protein that could not be purified, forcing a fresh start to the project by production of new mutants substituting phenylalanine for tryptophan instead of asparagine.
Michael Crowser (Advisor)
33 p.

Recommended Citations

Citations

  • Herron, L. (2003). Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1 [Undergraduate thesis, Miami University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1110916836

    APA Style (7th edition)

  • Herron, Lissa. Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1. 2003. Miami University, Undergraduate thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1110916836.

    MLA Style (8th edition)

  • Herron, Lissa. "Determining Which Tryptophan Residues Give Rise to Fluorescence Properties in the Metallo-Beta-Lactamase L1." Undergraduate thesis, Miami University, 2003. http://rave.ohiolink.edu/etdc/view?acc_num=muhonors1110916836

    Chicago Manual of Style (17th edition)