Hydroxamic acids are functional groups with the ability to strongly chelate metal ions found in the reaction centers of biologically important proteins including that of Tumor Necrosis Factor alpha Converting Enzyme (TACE)/(ADAM-17).  These hydroxamic acids are able to inhibit the enzymatic activities that are necessary for the normal progression of diseases such as HIV and cancer. One example is hydroxamic acids (Vorinostat) ability to block the release of the TNFalpha into the bloodstream of cancer and HIV patients thereby decreasing the inflammation response and slowing disease progression. This work sought to understand what modification surrounding the hydroxamic acid would be able to increase the overall binding affinity for metal chelation.  Differences in the inductive effects that surround the acids will be explored using ab-initio energy (DFT-B3LYP-631++G, and DFT-B3LYP-321-G) changes between apo/metal chelated molecules. These differences will seek to determine the best structural modification for improved hydroxamic acid design.