• Anna G

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.

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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.

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  • Anna G

Karissa Carter is a recent graduate of Norfolk State University in Norfolk, Virginia. She was accepted into a graduate program at the University of California, Davis where she will be pursuing her PhD in Chemistry starting Fall 2021. She is currently a researcher in Dr. Hairong Guan’s lab where she is investigating the synthetic pathway of a nickel complex that was formed from a tetradentate Schiff-base ligand. In general, a Schiff base is a compound with an imide functional group that contains an organic side chain on the nitrogen. Schiff-base ligands are called salen ligands if they are formed from salicylaldehyde and diamine derivatives. Salen ligands are unique in the formation of metal catalysts because they contain an interesting N2O2 donor set. Although they are typically easy to prepare, an unknown reaction occurred during the crystallization of a Ni(salophen) complex; a side chain was added to the imide nitrogen in the H2salophen ligand. To study this reaction, Karissa is synthesizing and reducing the H2salophen derivative formed from 2,4-di-tert-butylsalicylaldehyde and phenylenediamine. After forming the ligand, she will attempt to synthesize the Ni(salophen) complex. If successful, the nickel complex could potentially be a new catalyst.

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