Faculty Advisor

Hobey, William D.

Abstract

HIV-1 protease, an important catalyst in the maturation of HIV, can be blocked by inhibitor drugs. However, the protease is able to adapt by undergoing mutations in order to avoid being blocked. The purpose of this study was to understand the structure of HIV protease through a unique technique of tetrahedral simulations, as well as by calculating mutation stability changes and by creating van der Waals diagrams. Using these techniques, it was possible to understand interdependence among mutations as well as important amino acid residues involved in the movement of the protease. It was found that residues with higher rate of movement were more prone to mutation than residues which had less movement. Residues 13ILE and 15ILE moved the most in the nonligand protease structure. Typically, group interdependence of certain mutant residues was an important factor in allowing stability of mutations.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2003

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Chemistry and Biochemistry

Advisor Program

Chemistry and Biochemistry

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