Erin Gannon, Ohio University

Erin Gannon is a Rising senior at Ohio University in Athens Ohio, where she is studying Forensic Chemistry. This summer she is working under the guidance of Chethani Ruhunage in the Alvarez lab studying methods and tools of organic materials chemistry, and electrochemistry to understand nanometer-scale phenomena and invent solutions and technologies for neuroscience, monitoring water quality, and energy storage. Her assigned project this summer is based around an engineering concept that will hopefully be able to be used as an electrode array to further understand the dopamine influence in neuroscience. Specifically, she is focusing on utilizing nanofibers, polymer, and the creation of a mold to fabricate multiple electrode arrays at once. The outcome of this engineering project is to manually create multiple electrode arrays to make the detection of dopamine within human bodily fluid samples more efficient and easier to analysis. Dopamine detection in a human blood sample using this manually built electrode array will utilize cyclic voltammetry technique and less sample fluid then the commonly used open ended CNT fiber electrode. The cyclic voltammetry method will detect the dopamine amount in a blood sample allow the study of neurons to be conducted.

Sarah Mullen, College of Wooster

Sarah is a rising senior at The College of Wooster in Wooster, Ohio. This summer she is working in the Dima research lab, where she is computationally studying microtubule severing enzymes. These severing enzymes depolymerize and cause internal breaks in the microtubule lattice. Microtubule severing enzymes are responsible for the reorganization of microtubules in mitosis and meiosis, and they play important roles in cell motility, structure, and support. Sarah is working on two projects related to microtubule severing enzymes. The first project’s goal is to better understand the mechanism of microtubule severing enzymes. To do this, she is using coarse-grained modeling to see how the interaction strength of the severing enzyme to the microtubule affects the mechanism. For the second project she is looking at the monomers of the severing enzyme to better understand the possible secondary structural conformational changes. To accomplish this, she is taking protein trajectory data that was previously collected from molecular dynamics simulations and applying a type of unsupervised machine learning called clustering.

Zyrill Dela Cruz, University of Hawai'i Hilo

Zyrill is an upcoming junior majoring in chemistry at the University of Hawai'i at Hilo. In Dr. Kim's lab she is focusing on the structure and understanding of the mechanism of the human form of endonuclease SLXI and endonuclease SLX4. SLX41 by itself is inactive until it binds to the C-terminal region of SLX4. When the SLX1-SLX4 complex is formed, it is able to repair breaks in double-stranded DNA. Those broken double-stranded DNA can be caused by mechanical stress, chemical changes, metabolic reactions, chemotherapeutic drugs, and the process of meiosis. They go unrepaired, it can lead to gene deletion and chromosomal mutations. The SLX1-SLX4 complex is able to repair these breaks in DNA by cleaving near the branch point of branched DNA substrates. However, the mechanism of this actions is unknown. To learn more about this process, her goal is to purify SLX1 and SLX4 and have it be crystallized. The SLX1 and SLX4 complex is first expressed in Escherichia coli and followed by protein purification through affinity chromatography. Variables like affinity tags and pH are manipulated to find optimal condition at which SLX1 and SLX4 will purify. IF successfully purified, the endonucleases will be crystallized, and the results will be assessed to determine the structure and mechanism of action of the two proteins. This information will aid in further drug discovery.