The research focused on studying, at the molecular level, protein structure and function in Ras protein Cdc42 and its involvement in abnormal cell regulation signals that leads to oncogenesis. The specific purpose of the research was to examine possible new ways to liberate GDP from the protein of interest Cdc42Hs. Two experiments were tried to try to create apo-Cdc42Hs. First, the fluorescent analogue of GDP was degraded using Alkaline Phosphatase. Secondly, Cibracon Blue was used as possible affinity matrix due to its high affinity for ADP-binding proteins and because it binds to ADP it should also bind to GDP. Alkaline Phosphatase successfully degraded the fluorescent analogue of Cdc42 wt. which gives reason to believe that it would do the same in Cdc42Hs. With apo-Cdc42Hs there will be a better understanding of the structure of Cdc42Hs. which could potentially reveal insights on GDP dissociations and how this leads to cell proliferation.

Degradation of the nucleotide GDP from the ras protein Cdc42 wild type

241st National Meeting (2011)

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