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Helping Future Teachers Do History Through Digitized Primary Sources
The purpose of this study was to evaluate the impact of using the National Archives DocsTeach program on preservice teachers enrolled in a social studies methods course. Candidates completed a document-based question and a perception survey about history before completing one activity within the DocsTeach program for four classes. Anecdotal observations focusing on collaboration and engagement were collected during the unit. At the conclusion, participants completed another document-based question, a perception survey about history, and an exit interview. It was determined that the DocsTeach program had a positive impact on the participants’ historical thinking and perceptions of history
Empowering The Future: Cultivating Resilience in Adolescents
The concept of resilience has been explored in relation to various factors, including individual traits such as self-regulation, self-efficacy, and intrinsic motivation. External factors can also affect a student ability to be resilient such as support from family, peers, and school environments. A resilient student is one who can effectively cope with and adapt to challenges and setbacks during their academic journey. These students often share characteristics such as persistence, adaptability, critical thinking skills, and self- efficacy. These traits can collectively help students navigate educational difficulties and emerge stronger from their experiences
BC-73 Investigating the role of nonstructural protein 1 in the selective translation control of SARS-CoV viral RNA over host mRNAs
Nonstructural protein 1 (nsp1) from recent zoonotic coronaviruses (SARS-CoV-1, SARS-CoV-2, MERS-CoV) functions as a host shutoff protein that stalls host mRNA translation and triggers their degradation, successfully suppressing host gene expression. In contrast, viral RNA selectively escapes the effects of the two-pronged suppression mechanism and continues the synthesis of viral proteins due to the presence of stem-loop 1 (SL1) in the viral leader sequence. Recent structural analysis of nsp1 bound to the 40S ribosomal subunit suggests that the flexible C-terminal region of nsp1 binds to the 40S ribosome at the mRNA binding site by folding into two defined structures (alpha-helices); this interaction blocks host mRNAs from binding, stalling host mRNA translation. Meanwhile, the interaction between nsp1 and the viral leader sequence is thought to counteract that of nsp1-mediated translation suppression for the viral RNA. The exact nature of the selective control of translation has yet to be fully elucidated. Understanding these mechanisms more accurately is crucial to advance the current knowledge of similar host shutoff mechanisms in other viruses and uncover new anti-viral targets to control the spread of such viruses. Research in our laboratory is based on the hypothesis that the selective protection and preferential translation of viral RNA over host mRNA is based on nsp1’s ability to interact with RNA in both the nucleus and cytoplasm. We have previously established that nsp1 directly binds to viral SL1 sequence leading to two separate complexes, a small complex when nsp1 concentration is lower and a large complex when nsp1 concentration is significantly higher. These experiments were conducted by gel-shift assay using purified RNA and nsp1. By introducing mutations in the viral SL1, we mapped the interaction between nsp1 and viral RNA to understand the complex formation. However, when ribosomes were present, nsp1-SL1 complex formation changed into an even larger assembly.The objective of this project is to isolate and characterize the complexes formed between viral RNA, nsp1, and cellular extract (containing ribosomes) by mass spectrometry with a focus on clarifying the steps of viral RNA translation in the presence of nsp1. Our current results indicate that multiple cytoplasmic proteins bind the nsp1-SL1 complex but mutations in SL1 change its composition
BC-79 Removal and Desorption of Peanut (Arachis hypogaea) Allergens 1-3 Using Magnetic Nanoparticles for Application in Immunotherapy.
Peanuts are an inexpensive source of fats and proteins, but their health benefits are not available to people with an allergy (Bonku and Yu, 2020). The allergens of interest are the major allergens Ara h (Arachis hypogaea) 1-3 as they cause the most allergic reactions (Hurlburt et al., 2013). The most common peanut varieties in the US (Virginia, Jumbo Runner, and Spanish) were studied (Koppelman et al., 2016). Skinned and milled raw peanuts are defatted and proteins are extracted using carbonate buffer (pH 10.6). Magnetic iron oxide nanoparticles were coated with chitosan then tannic acid (MNP-CH-TA) and used to remove proteins from extracts. Trisaminomethane (Tris)/sodium chloride (NaCl) and sodium dodecyl sulfate (SDS) buffers were used to desorb allergens from the surface of particles. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), bicinchoninic acid (BCA) assay, enzyme-linked immunosorbent assay (ELISA) and attenuated total reflectance-Fourier transform infrared (ATR-FTIR) were used to evaluate adsorbed and desorbed proteins. Results from BCA assay show that MNP-CH-TA treated with phosphate buffer (pH 7.4) adsorbed more allergens than carbonate buffer (pH 10.6). The Jumbo Runner variety adsorbed most proteins, with a loss of 753.9 ± 29.1 µg protein per gram defatted peanut powder and the Virginia variety adsorbed the least, with 399.6 ± 145.7 µg protein per gram defatted peanut powder. According to ELISA results, SDS buffer desorbed more Ara h 3 from particles after contact with Jumbo Runner extract (93.89% [0.01 CV%]) compared to Tris/NaCl buffer (90.88% [20.29 CV%]). Future research will further focus on optimizing the allergen desorption process for application in allergen immunotherapy and particle reuse