BIOL 2083 : Exam 1 Potential Discussion Questions
Document Summary
Remember this is biochemistry and you must include molecular-level details not just general descriptions: consider the three amino acids below. Label all of the h-bond donors (d) and acceptors (a). The most common mutation associated with the disease is the change. These large differences in the charges and structure of these amino acids prevents them from working the same way. Transient assemetry in one atom will induce complementary assemmetry in another: the hydrophobic effect drives protein folding and also determines how proteins fold. The hydrophobic parts of the protein are on the inside where they are not in contact with water while the outside is hydrophilic: electrostatic interactions also play a part because different side chains have different charges. Like charges will repel and opposite charges will attract. This will contribute to how the protein is able to be arranged in each level of structure: proteins are flexible but conformationally restrained along their peptide backbone.
