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Nuclear Magnetic Resonance Spectroscopy in the Study of Protein Complexes

Bilinovich, Stephanie M
http://rave.ohiolink.edu/etdc/view?acc_num=akron1396871078

Abstract Details

2014, Doctor of Philosophy, University of Akron, Chemistry.
Nuclear magnetic resonance (NMR) spectroscopy is a versatile technique for the study of proteins and protein complexes. Simple experiments are utilized in the process of determining ligand binding and the binding interfaces in complexes can be mapped onto the known structures. In addition, the tertiary structure of the protein can be determined using different experiments. Two model proteins, human steroid receptor RNA protein (SRAP) and Brucella melitensis glutaredoxin (GRX) were used to study various protein to ligand binding events. GRXs are important proteins in the antioxidant system and have a CPYC active site that makes them possible targets for metal binding. NMR is a powerful technique for the qualitative study of metals binding interfaces in proteins. It also is powerful in the quantitative binding of metals to proteins through the determination of binding stoichiometry and the dissociation constant (Kd) for weakly bound systems. Human SRAP is a putative RNA binding protein that has been indicated to bind to its own mRNA. NMR was used to show that SRAP does not bind to its own mRNA. Both of these protein systems show that NMR is a potent method to study complexes and ligand binding to proteins.
Thomas Leeper, Dr. (Advisor)
Wiley Youngs, Dr. (Committee Member)
Claire Tessier, Dr. (Committee Member)
Christopher Ziegler, Dr. (Committee Member)
Amy Milsted, Dr. (Committee Member)
170 p.
Biochemistry
NMR; protein complexes; protein structure, GRX; SRA1 RNA; SRA1P

Recommended Citations

Citations

  • Bilinovich, S. M. (2014). Nuclear Magnetic Resonance Spectroscopy in the Study of Protein Complexes [Doctoral dissertation, University of Akron]. OhioLINK Electronic Theses and Dissertations Center. http://rave.ohiolink.edu/etdc/view?acc_num=akron1396871078

    APA Style (7th edition)

  • Bilinovich, Stephanie . Nuclear Magnetic Resonance Spectroscopy in the Study of Protein Complexes. 2014. University of Akron, Doctoral dissertation. OhioLINK Electronic Theses and Dissertations Center, http://rave.ohiolink.edu/etdc/view?acc_num=akron1396871078.

    MLA Style (8th edition)

  • Bilinovich, Stephanie . "Nuclear Magnetic Resonance Spectroscopy in the Study of Protein Complexes." Doctoral dissertation, University of Akron, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=akron1396871078

    Chicago Manual of Style (17th edition)

akron1396871078
271
© 2014, all rights reserved.
This open access ETD is published by University of Akron and OhioLINK.