HIV-1 protease is a significant target for the development of inhibitory drugs for the treatment of HIV-1. In order to expose the active site to the substrate, HIV protease displays significant movement in the flap region of the protease due to hydrophobic sliding. It has been proposed that by establishing a disulfide bridge in this region of the protease the conformational flexibility of the flap region to expose its active site will be restricted. To this end, a cysteine and alanine mutant has been created to test the feasibility of disulfide bridge formation in the flap regions. This study establishes that the single alanine and single cysteine mutations in the flap region do not affect the folding or binding ability of the protease significantly.

• 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

• Welch, Angelica Teresa

Publisher

• Worcester Polytechnic Institute

Identifier

• E-project-042910-113406

Advisor

• Heilman, Destin

Year

• 2009

Sponsor

• Schiffer Lab, University of Massachusetts Medical

Date created

• 2009-04-29

Resource type

• Major Qualifying Project

Major

• Biochemistry

Rights statement

• In Copyright