Proteins are broken down in the body and produce water, CO<sub>2</sub>, 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. Urea is known to denature proteins and this functionality continues to be a topic of great interest. Guanidine is another important nitrogen-containing molecule that is structural similar to urea and also plays important biological roles in the stabilization of proteins. 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. Here, we use Raman spectroscopy to study how urea and guanidine affects the hydrogen bonded network of water both in solution and when frozen out using Raman Under Nitrogen Spectroscopy (RUNS).

Raman spectroscopic and computational study of hydrogen bond interactions between urea, guanidine, and water

255th National Meeting (2018)

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