ThesisAuthors: Gong, Haipeng (2006)
Since the introduction of Pauling's groundbreaking =dell, numerous experiments have shown that hydrogen-bonded secondary structure is an important factor in protein folding. Under folding conditions, the linear polypeptide chain can form marginally stable elements of secondary structure on a rapid time scale. Such elements, which are in dynamic equilibrium with their respective coil states, interact with one another, further organizing and stabilizing the protein. We hypothesize that this latter step is rate limiting in the folding of a protein domain. To validate this idea, I tested whether the logarithm of the folding rate constant is linearly correlated with a protein's secondary structure content. The observed, large correlation coefficient is consistent with our hypothesis and ... 
