Abstract
Inosine-5’-monophosphate dehydrogenase (IMPDH), which is the rate-determining step of\r the guanine nucleotide biosynthetic pathway, is a target for anticancer, antibiotic, antiviral,\r and immunosuppressant drug development. Additionally, mutations in human IMPDH are\r correlated to inherited retinal degeneration. Previously, we discovered binding interactions\r between IMPDH and both ribosome and RNA polymerase in Escherichia coli. I designed\r several chromosomal IMPDH mutants to disrupt the binding between IMPDH and ribosome\r in order to locate the binding site. To increase the physiological relevance of this project, I\r began creating a collection of chromosomal IMPDH mutants, rather than using a plasmid-based\r approach. Future experiments will use affinity chromatography to purify selected\r mutant IMPDHs and check them for disruption of the interactions with RNA polymerase\r or ribosome. I have also developed several Python files to process IC50 data, producing a\r variety of visual and analytical interpretations of the data. One of the scripts takes in large\r IC50 data sets of inhibitors with enzymes from various species, and finds the minimal set of\r inhibitors needed to maintain the original hierarchical structure among the enzymes. My\r collection of five scripts allows investigators to process data sets within minutes that would\r have otherwise taken days or weeks to complete, or would not have been practical to attempt\r at all.