Faculty Advisor

Dempski, Robert E.

Abstract

Members of the ZIP family are essential for transition metal homeostasis as they regulate the cytosolic concentrations of zinc and/or iron. The human (h) ZIP4 membrane protein transports zinc into epithelial cells and has a central role in the absorption of dietary zinc. The subunit stoichiometry of hZIP4 is unresolved, but ab initio models suggest that hZIP4 forms a homodimer in the plasma membrane. Total Internal Reflection Fluorescence Microscopy (TIRFM) is a single molecule imaging technique that can be used to determine the subunit stoichiometry of membrane proteins by counting the photobleaching steps. TIRFM was used to determine the stoichiometry of hZIP4 on the plasma membrane. Analysis of these experiments indicates that hZIP4 forms dimers.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2016

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Chemistry and Biochemistry

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