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Date of Award


Document Type

Restricted Thesis: Campus only access

Degree Name

Bachelor of Science



First Advisor

Dr. Linda M. Boland


Reactive oxygen species (ROS) play important roles in cellular signaling. During oxidative stress conditions such as neurodegenerative disease, ROS can oxidize a variety of structures in neuronal and glial cells. Inwardly-rectifying potassium (Kir) channels are a subset of channels that contribute to the resting membrane potential of neurons and can possess extracellular cysteine residues that may be susceptible to extracellular oxidation. This study examines the potential for the ROS, hydrogen peroxide (H2O2), to interact with Kir channels through the use of homology modeling and two-electrode voltage clamp electrophysiology. It was determined that extracellularly-facing Cys149 within the pore region of Kir2.1 may interact with H2O2 to modulate current amplitude in Xenopus oocytes, but not in sponge (Aq) Kir which lacks the corresponding cysteine residue. By utilizing the cysteine-specific reagent, MTSEA, I also conclude that Cys149 is accessible extracellularly and that pretreating channels with 2-Aminoethyl methanethiosulfonate (MTSEA) prevents H2O2 current modulation.