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.

• 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

• Goller, Carlos C.

Publisher

• Worcester Polytechnic Institute

Identifier

• 02A007M

Advisor

• Argüello, José M.

Year

• 2002

Date created

• 2002-01-01

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright