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Master of Science in Applied Physical Science (M.S.)
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Thesis (open access)
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This work is licensed under a Creative Commons Attribution 4.0 License.
Department of Chemistry
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Proteins and their unique structures are important due to their involvement in every cellular task, but the protein can only function properly when it is in the correct fold. β-sheet peptides and collagen were observed via structural studies. Circular dichroism (CD) determines a protein’s secondary structure. WKWK, a beta-sheet peptide, is known to dissolve in aqueous solutions. However, WKWK was observed to precipitate out of deionized water. To investigate the cause of this precipitation, Inductively Coupled Plasma Mass Spectroscopy (ICP-MS) was used to determine the ion content of the water. Elevated sodium ion concentrations were found to disrupt the stabilizing cation-pi interaction of WKWK, causing unfolding. Both WKWK and collagen displayed random coil structures via CD, which is contrary to reported data.
Collagen was under investigation as a component of bio-based composites that could be utilized for bone or tissue replacement therapies. Collagen was desalted and an elution was collected from this process and analyzed via ICP-MS. The highest ion content detected in the elution was the sodium ion. With the removal of the sodium ions, structured and unstructured collagen samples were incorporated into tung oil composites to determine the effects of collagen fold on the composites. Differential Scanning Calorimetry (DSC) and Thermogravimetric Analysis (TGA) were used to determine thermomechanical properties of the composites to determine the potential for further material development.
Lorts, Aimee, "Investigation of the Effects of Ionic Interactions in Peptide and Protein Structure" (2017). Electronic Theses and Dissertations. 2609.
Research Data and Supplementary Material