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In 2008, Beese published her research on Candida albicans’ geranylgeranyltransferase-1 (GGTase-1) protein structure. Candida albican is an opportunistic pathogen commonly found in the human microbitoa. In immune compromised individual, C. albican result in infections that display resistance to anti-fungal therapies. The investigation and discovery of the structure of an GGTases-1 of Candida albicans provides more information for scientists to understand the protein’s importance in the survival of the pathogen and suggests its’ potential to be targeted for disease treatment.

While at Duke University in 2011, Beese, along with her colleague Eugene Wu, investigated the structural adaptation of DNA Polymerase observed during the recognition and correction of incorrect base pairing. Her findings included an intermediate state between the characteristic “open” and “closed” states of polymerase during DNA replication. This intermediary was termed the “Ajar” confirmation. Beese found that inserting an incorrect nucleotide into the growing DNA caused a bend in the helicase of the DNA polymerase. This finding suggests a mechanism by which polymerases are able to detect incorrect base pairing.

Beese had an integral role in identifying the mismatch repair mechanism through which hExo1 identifies DNA damage. In order to maintain the integrity of DNA, enzymes such as Human exonuclease 1 (hExo1) repair damages in DNA. Through her research, Beese found that the hExo1 enzyme binds the DNA near the site of mismatched pairing, and through exonuclease and endonuclease activity, the enzyme is able to assist in the identification and replacement of incorrect base pairs.