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
Copyright Statement
All authors have granted to WPI a nonexclusive royalty-free license to distribute copies of the work, subject to other agreements. Copyright is held by the author or authors, with all rights reserved, unless otherwise noted.
Accessibility
Unrestricted
Advisor Department
Chemistry and Biochemistry