Research Symposium
26th annual Undergraduate Research Symposium, April 1, 2026
William Blass Poster Session 3: 1:45 pm - 2:45 pm / Poster #93
BIO
I am an undergraduate student at Florida State University (FSU) majoring in Biological Science. I am originally from Pittsburgh, Pennsylvania, and developed an early interest in science through curiosity about human health and molecular biology. At FSU, I have gained hands-on experience in biochemical research, focusing on protein expression, purification, and enzymatic analysis.
My current research involves studying human guanylate-binding protein 5 (GBP5), where I use techniques such as affinity chromatography, ion exchange chromatography, size-exclusion chromatography, and malachite green assays to investigate protein function. Through this work, I have developed strong laboratory skills and a deeper understanding of protein biochemistry.
I plan to continue building my experience in research and apply my scientific background to future career opportunities in science and health-related fields.
Biochemical Characterization of Human GBP5
Authors: William Blass, Qian YinStudent Major: Biology
Mentor: Qian Yin
Mentor's Department: Cell and Molecular Biology Mentor's College: Weill Cornell Medical College Co-Presenters:
Abstract
Guanylate-Binding Protein 5 (GBP5) is an interferon-inducible GTPase involved in innate immune signaling, including inflammasome activation and host defense against intracellular pathogens. This study aimed to establish a robust expression and purification workflow for recombinant human GBP5 to enable downstream functional and structural analyses.
Human GBP5 was expressed in Escherichia coli using a pET-28a(+) system and purified through sequential affinity, ion-exchange, and size-exclusion chromatography to obtain pure, tag-free protein. Protease-mediated tag removal and metal chelation ensured elimination of residual contaminants and catalytic interference. The final preparation yielded soluble GBP5 suitable for biochemical analysis.
SDS-PAGE and chromatographic profiles confirmed purity and homogeneity.This purification framework provides a foundation for future studies investigating GBP5 GTPase activity, oligomerization dynamics, and its role in membrane-associated immune signaling.
Keywords: GBP5 Protein Purification GTPase Activity Size-Exclusion Chromatography Recombinant Protein Expression