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ULTRAFAST SPECTROSCOPIC AND DENATURANT STUDIES OF CYTOCHROME C

Reinhold, Benjamin M

Abstract Details

2014, Master of Science, Ohio State University, Chemistry.
Protein fluctuations are essential for protein function. Time resolved fluorescence allows us to measure energy transfer from a donor to acceptor. Cytochrome c is a flexible protein with one tryptophan and a heme moiety. Excitation of the tryptophan results in an energy transfer pair being formed. Systematic mutagenesis allowed us to examine the local environment in any area of the protein. Furthermore the use of the denaturant allows us to change the free energy difference between the folded and unfolded state. The effect of this free energy change on energy transfer was examined. Steady state measurements were also conducted to construct folding curves for individual mutants. The results were compared to current cytochrome c folding data, specially the foldon model of Walter Englander, and similar experiments on myogoblin, a more rigid protein.
Dongping Zhong (Advisor)
Thomas Magliery (Committee Member)
62 p.

Recommended Citations

Citations

  • Reinhold, B. M. (2014). ULTRAFAST SPECTROSCOPIC AND DENATURANT STUDIES OF CYTOCHROME C [Master's thesis, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1404257381

    APA Style (7th edition)

  • Reinhold, Benjamin. ULTRAFAST SPECTROSCOPIC AND DENATURANT STUDIES OF CYTOCHROME C. 2014. Ohio State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1404257381.

    MLA Style (8th edition)

  • Reinhold, Benjamin. "ULTRAFAST SPECTROSCOPIC AND DENATURANT STUDIES OF CYTOCHROME C." Master's thesis, Ohio State University, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=osu1404257381

    Chicago Manual of Style (17th edition)