Abstract
Understanding the forces that drive protein folding is essential for many of the central quests of structural biology including structure prediction, design and deciphering evolution. Nevertheless, we still have a rudimentary understanding of membrane protein folding energetics. I will describe tools we have developed for studying the factors that stabilize membrane proteins. Application of these methods suggests that packing forces, rather than hydrogen bonding, dominate membrane protein stabilization. Given the importance of dispersion forces, it is possible that membrane proteins might utilize packing more effectively than soluble proteins. We find that membrane proteins are not necessarily more efficiently packed, but manage to bury more surface area than soluble proteins. The results have implications for membrane protein evolution and their susceptibility to disease-causing mutations.
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