The research of my lab is focused on understanding the specificity of the aspartic proteinase family. This family includes the gastric enzymes pepsin and gastricsin, cellular enzymes cathepsin D and cathepsin E, enzymes from the malaria parasite, Plasmodium falciparum, and the retroviral enzymes such as HIV and FIV PR. We utilize site-specific mutagenesis as well as domain exchange to ascertain the effect on catalysis, and obtain structural information via crystallography or NMR. Given that we must have pure samples of fully functional proteins and because we are working with many mutant forms of recombinant proteins, we frequently solve problems and optimize protein folding. Our work on active site specificity has proved valuable in the process of drug design for targets involved in infectious diseases. |
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