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Functional Analyses of Human Serum Paraoxonase1 (HuPON1) Mutants Using Drop Coating Deposition Raman Difference Spectroscopy

Ying, Hua
http://rave.ohiolink.edu/etdc/view?acc_num=osu1284657860

Abstract Details

2010, Master of Science, Ohio State University, Chemistry.
We present work on the structural implications of specific mutants of Paraoxonase1 (PON1) G2E6, and the turnover rate upon bonding of the enzymes with paraoxon when compared to the wild-type enzyme by using vibrational spectroscopy. A new Raman spectroscopy called Drop Coating Deposition Raman (DCDR) is utilized in our work. The Raman band changes in the paraoxon/H115W system are in good agreement with computational calculations and are strong evidence of the formation of the paraoxon hydrolysis product, p-nitrophenol in the reaction system. The corresponsive turnover rates of G2E6 wild-type and its two mutants, H115W and H115T, are also observed in DCDR spectra.
Terry Gustafson (Advisor)
Thomas Magliery (Committee Member)
Chemistry
PON1; paraoxon; Raman; DCDR; Raman difference spectroscopy

Recommended Citations

Citations

  • Ying, H. (2010). Functional Analyses of Human Serum Paraoxonase1 (HuPON1) Mutants Using Drop Coating Deposition Raman Difference Spectroscopy [Master's thesis, Ohio State University]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=osu1284657860

    APA Style (7th edition)

  • Ying, Hua. Functional Analyses of Human Serum Paraoxonase1 (HuPON1) Mutants Using Drop Coating Deposition Raman Difference Spectroscopy. 2010. Ohio State University, Master's thesis. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=osu1284657860.

    MLA Style (8th edition)

  • Ying, Hua. "Functional Analyses of Human Serum Paraoxonase1 (HuPON1) Mutants Using Drop Coating Deposition Raman Difference Spectroscopy." Master's thesis, Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1284657860

    Chicago Manual of Style (17th edition)

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This open access ETD is published by The Ohio State University and OhioLINK.