Cu+-ATPases are a family of enzyme responsible for the transport of Cu+ across membranes. These ATPases receive Cu+ from a specific metallochaperone. Five unique CopA Cu+-ATPases (CopA1a, CopA1b, CopA2a, CopA2b, and CopA3) and two CopZ chaperones (CopZ1 and CopZ2) were previously discovered in Sinorhizobium Meliloti. This study sought to determine the specificity of each chaperone through the use of ClusPro software, which predicts protein-protein interaction through electrostatic calculations. The stoichiometric ratio of metals (Cu+ and Zn+) was also determined through atomic absorption spectroscopy. CopZ1 was predicted to be specific to CopA2a and CopA2b while CopZ2 is specific to CopA1a and CopA1b. CopZ1 and CopZ2 were each found to bind a single Cu+ ion and no Zn+ ions.

• 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

• Hall, Joshua Daniel

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-032316-215309

Advisor

• Argüello, José M.

Year

• 2016

Date created

• 2016-03-23

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright