Faculty Advisor

Argüello, José M.

Abstract

The target of this study was to examine one of the two known heavy-metal transporter P-type ATPase encoded by the prokaryote Archaeoglobus fulgidus. Efforts were focused on the functional characterization of CopA by testing the kinetics of this enzyme with and without the putative metal binding domain (MBD). The goal was to address questions regarding the significance of the MBD in the translocation of ions across biomembranes and the effects of several biochemical parameters on ion transportation. Results indicate that the truncated protein continues to be active and has a higher affinity for silver than intact CopA. This behavior may suggest that the putative metal binding domain plays a role in regulation.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2002

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Chemistry and Biochemistry

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