Faculty Advisor

Heilman, Destin

Abstract

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.

Publisher

Worcester Polytechnic Institute

Date Accepted

April 2010

Major

Humanities and Arts

Major

Biochemistry

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Chemistry and Biochemistry

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