Discussion: Many of our most important enzyms, hormones, and chemical process are all made possible by the presence of protiens. We can build protiens in our bodies or injest them in the food we eat. Tryptophane and tyrosine were some protein amino side chains that we specifically identified in the lab. Some everyday foods that contain high contents of tryptophane are egg whites, fish, and seeds. While some common foods that are high in tyrosine are cheese, milk, and tofu. The samples experimented on in the lab also had contents of tryptophane and tyrosine. The skim, 2% milk and the powdered protein contained both Tryptophane and tryrosine while the Gelatin contained Tyrosine. To see the specific amounts per 100grams, refer to Table 2 in the results section. …show more content…
An obvious reason causing the discrepancies was that the lab equipment used could have easily been contaminated from the previous lab before and could have affected the results of our lab. If there was left contaminants in the beaker and lab equipment it could have given us different results than was is expected. Also the measurement used could have been inaccurate, therefore producing the discrepancies Both the Biuret test and the Xanthoprotreic test were used in today’s lab procedures but assuming that the vast majority of protein contained one or both tyrosine and tryptophane we would be able to replace the biuret test in Part 1 in detecting protein in a substance with the Xanthoproteic test, This test would identify the tyrosine and tryptophane in a substance only difference is with this test it would turn samples with protein in it a yellow colour. When albumin is denaturing the peptide bonds linking adjacent amino acids are not hydrolyzed. In order to break down any protein primary structure we would need to use both heat and acid. The secondary, tertiary, and quatranary levels of protein structure will be altered but not the primary