Found 4 projects
Oral Presentation 2
1:15 PM to 3:00 PM
- Presenter
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- Yubin Li, Sophomore, Computer Science, Shoreline Community College
- Mentor
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- Lauren Bryant, Information School, Shoreline Community College
- Session
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Session O-2P: Large Language Models: Engineering and Social Requirements
- CSE 305
- 1:15 PM to 3:00 PM
Addressing bias in artificial intelligence (AI) and machine learning (ML) systems is crucial for ensuring fairness, transparency, and ethical integrity. This study introduces a pioneering interdisciplinary approach, blending advanced computational methods with social sciences insights to tackle the multifaceted nature of bias. Through a mixed methods strategy that combines quantitative and qualitative data, we scrutinize algorithmic outcomes and conduct different case studies of stakeholders—developers, users, and communities affected by AI/ML biases. Our initial findings indicate that bias transcends technical boundaries, manifesting as a complex socio-technical dilemma that demands both algorithmic adjustments and societal reforms. We highlight specific biases, such as gender and racial disparities in recruitment algorithms and facial recognition technologies, underscoring the critical need for our research. To address these biases, we propose adopting data enhancement techniques, fairness-focused learning algorithms, and promoting explainable AI practices. Inspired by influential figures like Joy Buolamwini, founder of the Algorithmic Justice League, and Cathy O'Neil, author of Weapons of Math Destruction, we emphasize the importance of inclusive datasets and critically examining opaque algorithms. Our future efforts concentrate on developing comprehensive guidelines to reduce AI/ML biases and exploring the broader societal impacts of establishing unbiased AI and ML systems. By cultivating more equitable and ethical AI and ML frameworks, our research aims to meet the diverse needs of global communities, setting a new standard for responsible AI development.
Poster Presentation 3
2:15 PM to 3:30 PM
- Presenter
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- Johnathon Whitacre, Sophomore, Archeology , Shoreline Community College
- Mentor
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- Lauren Bryant, Information School, Shoreline Community College
- Session
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Poster Session 3
- MGH Commons West
- Easel #19
- 2:15 PM to 3:30 PM
Poster Presentation 4
3:45 PM to 5:00 PM
- Presenter
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- Lia Barrow, Senior, Biochemistry
- Mentors
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- Lauren Rajakovich, Chemistry
- Jayden Eppley, Chemistry
- Session
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Poster Session 4
- HUB Lyceum
- Easel #97
- 3:45 PM to 5:00 PM
Gastrointestinal symptoms are a common comorbidity of autism spectrum disorder (ASD), and individuals with the disorder tend to have a distinct gut microbial community composition and circulating metabolomes. My work in the Rajakovich Group focuses on a gut-derived metabolite, 4-ethylphenolsulfate (4-EPS), found in higher abundance in ASD mouse models and children with ASD. 4-Ethylphenol (4-EP), its precursor, is produced by gut microbiota before host-mediated sulfation, but the microbial biosynthetic pathway is unknown. A proposed metabolic pathway suggests the microbial stepwise conversion of plant-derived complex polysaccharides to 4-EP. My project goal is to identify a gut microbial enzyme responsible for the first step of this proposed pathway: a hydroxycinnamoyl esterase. I used literature searches and bioinformatics tools to identify characterized bacterial cinnamoyl esterases and candidate enzymes. I designed plasmids for two candidate enzymes (both from E. faecium, known to colonize the gut) and one characterized esterase (from L. plantarum). Currently, I am working on expressing the proteins in E. coli cells and purifying them by affinity chromatography. Once purified, I will assess the enzymes for their anticipated cinnamoyl esterase activity by incubating them with dietary hydroxycinnamic acid esters and detecting products with high-performance liquid chromatography (HPLC) and UV/Vis spectroscopy. Since the candidate enzymes are homologs of confirmed esterases and have conserved catalytic motifs, I hypothesize that they will have hydrolytic activity. If correct, I will see consumption of the substrate (no detection) and detect the anticipated products. Positive results from these assays would complement ongoing work by the lab to identify other E. faecium enzymes in this proposed pathway. Though it is debated if 4-EPS is causal to the disorder or simply a biomarker, elucidating its biosynthetic pathway and studying the biochemistry of gut microbes will contribute to detangling the gut’s role in ASD.
- Presenter
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- Tanner Olson, Junior, Biochemistry
- Mentors
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- Lauren Rajakovich, Chemistry
- Rachelle Stowell, Chemistry
- Session
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Poster Session 4
- HUB Lyceum
- Easel #98
- 3:45 PM to 5:00 PM
The modification of tRNA plays a significant role in the efficiency and accuracy of translation during protein synthesis. A modification that plays a direct role in reading cognate codons of mRNA in E. coli is the 5-oxyacetic acid methyl ester (mcmo5) modification. This modification occurs on the uracil base at position 34 (U34). The biosynthetic pathway of this modification is initiated via a hydroxylation reaction. Previous in vivo studies demonstrate the enzyme TrhP, tRNA hydroxylation protein, performs this hydroxylation reaction in anaerobic conditions. No in vitro work has been done to study this enzyme and its mechanistic function. TrhP is known to coordinate an iron-sulfur cluster, a metallic cofactor known to contribute to a variety of critical cellular processes, however, the necessity of an iron-sulfur cluster for a hydroxylation reaction is unique to this newly discovered protein family. The goal of this research project is to spectroscopically characterize TrhP’s iron-sulfur cluster to understand the importance of the FeS cluster. Site-directed mutagenesis is utilized to study the coordination of the iron-sulfur cluster. Changes to iron-sulfur cluster coordination are monitored via UVVIS, electron paramagnetic resonance (EPR), and colorimetric assays. These experiments determine how the loss of cysteine, a known iron-sulfur cluster ligand, impacts the iron-sulfur cluster coordination. Coordination of a [2Fe2S] cluster by 4 conserved cysteines is expected, and UVVIS data agrees with that hypothesis. Colorimetric assays show the cysteine to alanine mutants contain less iron than wild-type TrhP, indicating each cysteine has a significant role in cluster binding. Learning more about the specific coordination will establish the site of cluster-binding within TrhP and shed light on the cluster’s role in TrhP’s stability, geometry, and redox properties which all contribute to the enzyme’s modification activity.