Year

2000

Degree Name

Doctor of Philosophy

Department

Department of Chemistry

Abstract

The reverse transcriptase (RT) enzyme of the human immunodeficiency virus is an attractive target for rational drug design as it is an essential and unique enzyme in the viral life cycle. RT can be inhibited by non-nucleoside inhibitors acting at an allosteric binding pocket (NNIBP). The inherent flexibility of the enzyme has made the study of the mechanism(s) of its functions and inhibition by non-nucleoside inhibitors difficult and ambiguous. Furthermore, this flexibility in the NNIBP has made it difficult to characterise the binding pocket for rational drug design.

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