To study the comparison between protein unfolding and protein aggregation in the presence of chemical denaturing agents.
In experiment 8 and 9 we have seen that how a protein can go from a folded to an unfolded state at extreme environmental conditions (high temperature or presence of other chemical ). At extreme conditions intramolecular bonds are broken and the protein molecule gains a deformed shape. But in a protein solution, in the unfolded state, proteins may form intermolecular bonds and can aggregate among themselves. Whether a protein will aggregate or not that depends on the environment.
So to study the characteristics of the protein in the unfolded state it is important to know whether the protein has undergone aggregation or not. CD spectroscopy provides a nice way to find out whether aggregation is taking place at the unfolded state.
In this experiment we will study the method to determine aggregation from CD spectroscopy. And will try to determine whether aggregation is happening in two different samples of Rhodopsin.