Faculty Advisor

Dempski, Robert E.

Abstract

Zinc is required for cellular homeostasis. When the concentration of zinc is not properly regulated pathological conditions develop. However, the mechanism of zinc transport across cellular membranes is not well-understood. The human (h) ZIP4 protein functions to increase the intracellular zinc concentration. When hZIP4 is mutated, acrodermatitis enteropathica, a zinc deficiency disease can develop. In this study, a fluorescence based assay is used to measure zinc binding affinity of the intracellular loop between transmembrane domains three and four (M3M4) of hZIP4. An analysis of our results reveal that histidine residues within M3M4 bind zinc with high affinity and M3M4 undergoes a conformational change upon zinc binding.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2014

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemistry and Biochemistry

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