FYRE in STEM 2023

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    Survey on the acceptability of a fetal monitoring device
    (Wichita State University, 2023) Brake, Anna; Keene Woods, Nikki
    Pregnant mothers living in rural areas are faced with reduced access to adequate maternal and fetal healthcare, leading to disparities in delivered care and contributing to increased adverse birth outcomes for mothers and babies. Using remote monitoring may help mitigate these issues. This project focuses on piloting a survey that will allow pregnant mothers to provide their input to the design process of a wearable fetal echocardiogram (fECG). This device will allow continuous monitoring of fetal health and the communication of this information to healthcare professionals. The survey includes 30 questions evaluating participant demographics and using a five-point Likert scale to determine the acceptability of using a wearable medical device during pregnancy. A convenience sample of eighteen women of childbearing age (18-49) was used for the pilot survey, meaning that women who were easiest to access for the researchers were surveyed. At the end of the survey, participants were asked follow-up questions concerning the survey methodology. Results were analyzed using descriptive statistics, and qualitative methods were used to summarize the main themes of the open-ended questions. All surveys in the pilot were taken online; when asked about preferred method of response, participants indicated that they would rather take the survey online, rather than verbally or on paper. According to participant feedback, the survey was easily understood, but several terms used in the survey need to be better defined. The project goal is to refine and fine-tune the survey to maximize participant cooperation and comprehension, as well as the quality of the data gathered in order to implement the survey among a sample size of 200 pregnant mothers in the summer of 2023.
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    Modelling the actin-myopalladin complex using crosslinking mass spectrometry
    (Wichita State University, 2023) Meuli, Rose Marie; Ajiboye, Oluwatosin; Beck, Moriah R.
    Myopalladin is an actin-binding protein that has recently been discovered in striated muscle tissue. Like its family members myotilin and palladin, myopalladin contains immunoglobin (Ig) domains that participate in actin binding. Myopalladin acts to stabilize actin and limit actin polymerization, but mutations in myopalladin have been linked to cardiomyopathy. A model of myopalladin's structure would provide a better understanding of this protein's role in cardiomyopathy. Therefore, the Beck lab has conducted an experiment to determine the structure of the myopalladin-actin complex and compare that structure with the better-known familial proteins palladin and myotilin. Like palladin, myopalladin's Ig3 domain has been identified by the Beck Lab as the minimum site required for binding to actin. The Ig3 domain of myopalladin was first crosslinked with filamentous (F-) actin using various chemical crosslinkers to create covalent bonds between the two proteins, thus trapping them in the complex. The crosslinked proteins were separated and visualized using an SDS-PAGE gel and DMTMM was determined to result in the most crosslinks between Ig3 and F-actin. The SDS-PAGE gel bands containing the Ig3-actin complex were then sent for crosslinking mass spectrometry (XL-MS) analysis. The results from the XL-MS will provide us with precise fragment masses that can be used to determine which amino acids from each protein are in close proximity. This data will then be used to determine a structural model of myopalladin via the use of programs such as P2-Link and HADDOCK. Once the myopalladin-actin complex has been modelled, the actin-binding sites can also be located. This information will provide insight into the actin-myopalladin interaction, which can then be used in comparison to palladin and myotilin to increase overall knowledge of these Ig-domain-containing proteins. Overall, the data collected in this experiment has the potential to be crucial for the better understanding of cardiomyopathy.
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    Wichita State University carbon footprint analysis
    (Wichita State University, 2023) McClelland, Stewart; Ahmed, Ikramuddin
    In the modern age, we are growing more aware of the limited time and resources this planet has and that we must take steps to prevent this. As a leader in innovation, we should also progress our efforts to combat the ongoing climate crisis. This research's main intent is to update the carbon footprint in respect to Scope 2 emissions of Wichita State University (WSU) from a previous study in 2019. Scope 2 will include the emissions produced through purchasing of utility power; electricity and natural gas bought from our providers. To calculate our emissions, we will catalog our usage of each utility, in kWh and MCF (1000 cubic feet) respectively, over 2022, and then multiply it by the emissions profile as reported by the Energy Information Administration. Once collected, we converted our usage information into kg CO2. Our results show that WSU Scope 2 emissions in the year 2022 produced 33,710,218.191 kg of CO2, approximately 2 million kg more than in 2019. Overall, there was a significant increase in emissions from electricity usage but with a decrease in gas usage. Nonetheless, putting us enroute to the average of producing just over 52,000 MT of CO2. This data will provide valuable insight on how to address campus carbon emissions and general energy usage to potentially help lower costs. This will help to promote awareness of carbon emissions in our lives and campus to better combat this increasingly large epidemic. Also, this study should be used for future revisions of Wichita State's carbon footprint as was the intention of the previous research study.
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    Relationship between flexibility and tongue muscle performance in healthy young adults
    (Wichita State University, 2023) Fernandez, Jennifer; Khan, Zainab; VanRavenhorst-Bell, Heidi A.
    Tongue muscle performance (e.g., tongue strength, tongue endurance) is essential for completing everyday tasks (i.e., swallowing, maintaining upper airway patency) and maintaining good health. Skeletal muscle has been shown to have better functional performance with increased flexibility. Knowing the tip of the tongue is connected to the tip of the toes through a series of connected fascia, tongue muscle performance may be impacted by skeletal muscle flexibility. This study sought to determine whether tongue muscle performance measures differ based on skeletal muscle flexibility measures. Data collection is currently active with an anticipated total of 40 healthy young adults (18+ years of age). Participants will complete one DARI assessment for range of motion analysis of skeletal muscle flexibility, three trials of tongue muscle strength, and one trial of tongue muscle endurance in both the anterior and posterior tongue region. Analyses will include descriptive statistics and a Pearson's Product Correlational Coefficient. All analyses will be set at an ? = 0.05. Based on current literature it is anticipated that tongue muscle performance will have a positive linear relationship with skeletal muscle flexibility. Such findings may suggest the inclusion of skeletal muscle stretching within current lingual therapy practices to promote healthier lingual performance.
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    War on cancer: Development of the covalent inhibitor on KRASG12D
    (Wichita State University, 2023) Wang, Jia Wen; Abijoye, Emmanuel; Wu, Haifan
    Mutations in the KRAS protein, such as G12C and G12D have been linked to many types of cancers including lung, colorectal, and pancreatic. Small molecules specifically targeting KRASG12C have been found to effectively bind to this protein to disable the protein and cease uncontrolled cell growth. Using this small molecule has led to successful cancer treatments with this cysteine (G12C) mutation. However, no such small molecule has been synthesized that can covalently bind to the aspartate (G12D) mutation to disable this protein, even though KRASG12D is the more common form of the KRAS mutations. Our overall goal is to synthesize a small molecule to target the Asp12 on the KRASG12D mutation using 2H-azirine. We have successfully purified three constructs of the KRAS protein: KRAS wild type, KRASG12C, and KRASG12D as well as incorporated GDP in each construct. GDP-bound KRAS is inactive. Small molecules targeting and maintaining this KRAS state can reduce cell proliferation. We are in the process of synthesizing the inhibitor to covalently label Asp12. If successful, this small molecule inhibitor would create opportunities for treatments of KRASG12D mutations.