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.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Doyon, Brian Ronald

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-041514-213815

Advisor

• Dempski, Robert E.

Year

• 2014

Date created

• 2014-04-15

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright