Encapsulation and Protein Stability

With this award, the Chemistry of Life Processes Program in the Chemistry Division funds Dr. Gary J. Pielak from the University of North Carolina-Chapel Hill for studies on how proteins behave when 'confined' to small spaces. The term confinement refers to isolation of the protein in a cavity roughly the size of the protein itself. This is how many proteins find themselves when inside of cells. Such confinement can affect the behavior of proteins and enzymes. The project is determining how confinement affects protein behavior during synthesis, misfolding, turnover and transport. This information is important to industrial applications such as enzyme stabilization. This research is also expanding efforts to reach underrepresented undergraduates by teaming up with the UNC Scholars' Latino Initiative.

This project is determining how confinement (isolation of the protein in a cavity roughly the size of the protein itself) affects protein behavior during synthesis, misfolding, turnover and transport. This information is important to industrial applications such as enzyme stabilization. The research is being accomplished by using a fluorine-labeled, metastable globular protein capable of reversible two-state folding that is entrapped in a unique system of reverse micelles. 19F NMR is being used to assess not only the free energy, but also the enthalpy and the entropy of unfolding. Structural effects of confinement also are being assessed.