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STRUCTURAL HEALTH MONITORING OF FIBER REINFORCED COMPOSITE STRUCTURES UNDER HIGH VELOCITY IMPACT LOADS

Description
This thesis encompasses research performed in the focus area of structural health monitoring. More specifically, this research focuses on high velocity impact testing of carbon fiber reinforced structures, especially plates, and evaluating the damage post-impact. To this end, various non-destructive evaluation techniques such as ultrasonic C-scan testing and flash thermography…

This thesis encompasses research performed in the focus area of structural health monitoring. More specifically, this research focuses on high velocity impact testing of carbon fiber reinforced structures, especially plates, and evaluating the damage post-impact. To this end, various non-destructive evaluation techniques such as ultrasonic C-scan testing and flash thermography were utilized for post-impact analysis. MATLAB algorithms were written and refined for the localization and quantification of damage in plates using data from sensors such as piezoelectric and fiber Bragg gratings sensors. Throughout the thesis, the general plate theory and laminate plate theory, the operations and optimization of the gas gun, and the theory used for the damage localization algorithms will be discussed. Additional quantifiable results are to come in future semesters of experimentation, but this thesis outlines the framework upon which all the research will continue to advance.
ContributorsMccrea, John Patrick (Author) / Chattopadhyay, Aditi (Thesis director) / Borkowski, Luke (Committee member) / Barrett, The Honors College (Contributor) / Mechanical and Aerospace Engineering Program (Contributor) / Department of Military Science (Contributor)
Created2015-05
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Expression, Purification, and Electron Microscopic Analysis of the Rubisco-Rubisco Activase Complex

Description
Ribulose-1,5-bisphosphate carboxylase/oxygenase enzyme (Rubisco) is responsible for the majority of carbon fixation and is also the least efficient enzyme on Earth. Rubisco assists 1,5-ribulose bisphosphate (RuBP) in binding CO2, however CO2 and oxygen have similar binding affinities to Rubisco, resulting in a low enzymatic efficiency. Rubisco activase (Rca) is an…

Ribulose-1,5-bisphosphate carboxylase/oxygenase enzyme (Rubisco) is responsible for the majority of carbon fixation and is also the least efficient enzyme on Earth. Rubisco assists 1,5-ribulose bisphosphate (RuBP) in binding CO2, however CO2 and oxygen have similar binding affinities to Rubisco, resulting in a low enzymatic efficiency. Rubisco activase (Rca) is an enzyme that removes inhibiting molecules from Rubisco’s active sites, promoting the Rubisco activity. The binding of Rubisco and Rca stimulates a high-rate of carbon fixation and lowers the overall CO2 concentration in the atmosphere. To study the interaction between the two complexes, Rubisco was extracted from baby spinach (Spinacia oleracea) and purified using anion-exchange chromatography and size-exclusion chromatography. Rca was designed to use a recombinant gene and overexpressed in Escherichia coli (E. coli). The purified proteins were verified using SDS-PAGE. The two proteins were assembled in vitro and the interaction of the protein complex was stabilized using glutaraldehyde cross-linking. The samples were then deposited on a carbon-coated electron microscopy (EM) grid, stained with uranyl formate, and observed under a transmission electron microscope (TEM). The ultimate goal is to image the specimen and reconstruct the structure of the protein complex at high resolution.
ContributorsHart, Hayden (Author) / Chiu, Po-Lin (Thesis director) / Redding, Kevin (Committee member) / Van Horn, Wade (Committee member) / Barrett, The Honors College (Contributor) / School of Molecular Sciences (Contributor) / Department of Military Science (Contributor)
Created2022-05