Author

Krystal T. Do

Publication Date

5-5-2017

Document Type

Dissertation/Thesis

First Advisor

Horn, James R.

Degree Name

B.S. (Bachelor of Science)

Department

Department of Chemistry and Biochemistry

Abstract

The characterization of the binding properties of the Zinc ion, a metal cofactor, for the IspF enzyme can reveal details of critical interactions that allows to better understand IspF function. The use of Isothermal Titration Calorimetry (ITC) was used to determine the binding affinity of the Zn2+ cofactor to the IspF enzyme. A sample of IspF was titrated with a Zinc solution, using a Zinc to Buffer titration as a control. This was done to isolate ligand and protein interactions from the interference of buffer solution. The titration of the Zn2+ cofactor can reveal insight into the binding thermodynamics with Burkholderia pseudomallei IspF. Further studies will be carried out against another IspF sample from Escherichia coli, as well as other 2+ metal ions like Magnesium (Mg2+) and Calcium (Ca2+).

Language

eng

Publisher

Northern Illinois University

Rights Statement

In Copyright

Rights Statement 2

NIU theses are protected by copyright. They may be viewed from Huskie Commons for any purpose, but reproduction or distribution in any format is prohibited without the written permission of the authors.

Media Type

Text

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