Study membrane protein folding in the native bilayer environments
Advisor: Yu-Chu Chang
Location: Max Planck Institute for Biology
The protein folding problem and stability are fundamental studies that serve as a hub for many other researches, such as mutation-disease relations, structural prediction of protein, and protein design. However, membrane proteins are largely bypassed in studying protein folding problems as membrane proteins often are hard to purify, tend to aggregate, and, therefore, are challenging to study. In this study, new strategies and techniques will be developed to study the membrane protein problem.
In this project, bacteriorhodopsin (bR) will be used as a model membrane protein for us to develop new methods for investigating membrane protein folding and stability. As shown in the figure, steric trapping and clipped trapping techniques utilize the coupling of the folding of the target membrane protein to a binding event. The binding of another soluble protein can drive the folding/unfolding of the membrane protein. Different lipid-protein environments, such as liposomes, bicelles, and nanodisks, will also be utilized to understand the folding properties of membrane protein in a physiological lipid bilayer environment and to systematically study the lipid effects on the membrane protein stability.
More information about the research of Yu-Chu Chang and a selection of recent publications can be found on his faculty page.
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Application deadline: 27 January 2025