The catalytic cycle of Na, K-ATPase enzyme has been described in great detail, but the events occurring at the molecular level to perform the energy-coupled ion transport are unknown. To approach this problem we performed site-directed mutagenesis of transmembrane helixes H5, H6 and the loop connecting them. A few residues were individually replaced by cysteine. In order to separate heterologously expressed protein from the endogenous proteins, Histidine-tag was introduced to some of the cysteine mutants. Resulting mutants were then stable expressed in COS cells.

• 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

• Dhimitri, Elda

Publisher

• Worcester Polytechnic Institute

Identifier

• 01D164M

Advisor

• Argüello, José M.

Year

• 2001

Date created

• 2001-01-01

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright