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Cooperativity of Protein Folding
The folding and unfolding of proteins is cooperative in nature. But what exactly does that mean? Under denaturing conditions, such as a high temperature, part of the protein becomes unstable. This unstable segment, because it interacts with other parts of the protein via non-covalent interactions, begins to destabilize another segment in the protein. This second segment in turn destabilizes a third segment in the protein and this process continues until the protein has been completely denatured. In this manner, segments of the protein cooperate with one another to unfold the protein. The same can be said about the reverse (folding) process. If we plot the percent denatured vs temperature, we will see a sigmoidal curve. This curve shows that as we increase the temperature, there is a sharp transition from the folded, native state to the unfolded, denatured state. This is a result of protein cooperativity. Generally, during the folding or unfolding process, the protein follows a partially-defined pathway that consists of energy-specific intermediate states
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