Honors Theses
Date of Award
2018
Document Type
Undergraduate Thesis
Department
Chemistry and Biochemistry
First Advisor
Nathan Hammer
Relational Format
Dissertation/Thesis
Abstract
Proteins are broken down in the body and produce water, CO2, and ammonia as by-products. Ammonia is toxic to cells, making it a priority to be excreted. Urea is the key route for the transportation of ammonia out of the body and is the main component of urine. Guanidine is another important nitrogen-containing molecule that is structural like urea and plays important biological roles in the stabilization of proteins. Guanidine hydrochloride and Urea are known to denature proteins and this functionality continues to be a topic of great interest. Urea and guanidine contain many hydrogen bonding sites and interactions with water are important to their biological functionality and their abilities to affect protein stability. Trimethylamine N-oxide (TMAO) is known to counteract the effects that urea and guanidine hydrochloride have at destabilizing proteins. Here, we use Raman spectroscopy to study how urea, guanidine hydrochloride, and TMAO affect the hydrogen bonded network of water both in solution at room temperature and in a frozen crystal state. The experiment confirmed previous research that showed a blue shift in the HNH bending region of urea when TMAO was added. Raman spectra of guanidine hydrochloride and TMAO was found to have two different blue shifts in the HNH bending region. Another perspective result for future research is that the low temperature Raman spectra of urea water was found show multiple peaks.
Recommended Citation
Kamischke, Andrew, "Raman Spectroscopic and Computational Study of Hydrogen Bond Interactions between Guanidine Hydrochloride, Trimethylamine N-oxide (TMAO), Urea, and Water" (2018). Honors Theses. 64.
https://egrove.olemiss.edu/hon_thesis/64
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