Access Type
Open Access Thesis
Date of Award
January 2011
Degree Type
Thesis
Degree Name
M.S.
Department
Biochemistry and Molecular Biology
First Advisor
Timothy L. Stemmler
Abstract
Iron is a micronutrient that acts as a cofactor in many prosthetic groups involving itself in almost every biological process. Iron is the key component in our body fluid, flowing in our veins all the time. Iron deficiency disorders affects more than 9 million people worldwide. Similarly, a high level of iron is associated with various disorders which suggest that in order for body to function properly level of iron should be tightly regulated. Many iron binding proteins help in maintaining cellular iron homeostasis by keeping iron in reduced form.
Working on the hypothesis that Poly (rC) Binding Protein family serve as iron chaperone, research presented here shows that PCBP2 binds ferrous iron with micromolar binding affinity. The structural data on PCBP2 shows that thus bound iron is in 6-coordinate O/N ligand environment. Data presented here characterizes PCBP2 as a dimeric protein, with high helical content. Characterization of PCBP2 will serve as a base for exploring the roles of PCBP2 in cellular iron homeostasis.
Recommended Citation
Ghimire-Rijal, Sudipa, "Characterization of poly (rc) binding protein (pcbp2) and frataxin" (2011). Wayne State University Theses. 71.
https://digitalcommons.wayne.edu/oa_theses/71