Yu-Chu Chang

Membrane protein folding, stability, and functions

Max Planck Institute for Biology Tübingen
Adjunct faculty in: IMPRS

Vita

• Ph.D. in Biophysics and Biochemistry, Duke University (2009)
• Postdoctoral training, University of California Los Angeles (2010-2015)
• Project Assistant Professor, Taipei Medical University (2015-2016)
• Assistant and Associate Professor (2017-2024), Department of Biochemistry and Molecular Cell Biology, Taipei Medical University
• Project Leader at MPI for Biology Tübingen (since 2025)

Research Interest

Develop novel techniques to investigate membrane protein folding and stability

Our research focuses on investigating the biophysical and biochemical properties of helical membrane proteins, particularly examining their folding stability and kinetics. We develop new methods to study the stability of membrane protein in the lipid bilayer and lipid disc conditions.

Bacteriorhodopsin (bR) is used as the model membrane protein for us to develop different new methods. Steric trapping and clipped trapping techniques utilize the coupling of the folding of the target membrane protein to a binding event. The folding/unfolding event of the membrane protein can be driven by the binding of another soluble protein. These techniques aim to understand the folding properties of membrane protein in a more physiological lipid bilayer environment rather than denaturant-induced folding/unfolding conditions.

Study the virulence-related proteins of Salmonella.

• Wzx: This integral membrane protein is involved in the lipopolysaccharide (LPS) biosynthesis process of gram-negative bacteria and serves as a lipid-linked oligosaccharide flippase in the pathway.
• YqiC: Through the protein-protein interaction studies, we found out YqiC’s function is tightly related to the energy protein in the bacteria, specifically in the electron transport chain (ETC).

Using combinatorial approaches, we explore the structural characteristics, functional mechanisms, and interaction networks of these proteins. Since the knock-out strains of these genes significantly affect the colonization and invasion ability of Salmonella, they are potential drug targets for the future development of novel antibiotics.

Available PhD Projects

• Study membrane protein folding in the native bilayer environments
• Novel proteins that affect Salmonella virulence

Selected Readings

• Chang YC, Cao Z, Chen WT, and Huang WC, “Effects of Stand-alone Polar Residue on Membrane Protein Stability and Structure”, BBA-Biomembranes 2024 Jun; 1866(5): 184325.
• Kuo CY, Tay R, Lin HC, Juan SC, de Ulzurrun GV, Chang YC, Hoki J, Schroeder F, and Hsueh YP, “The nematode-trapping fungus Arthrobotrys oligospora detects prey pheromones via G protein-coupled receptors,” Nature Microbiology 2024 Jul; 9(7): 434 1738-1751
• Huang WC, Chen WT, Chen YC, Fang SB, Huang TW, Chang PR, and Chang YC, “Salmonella YqiC exerts its function through an oligomeric state”, Protein Sci. 2023 Oct; 32(10): e4749.
• Chang YC and Bowie JU, "Measuring Membrane Protein Stability under Native Conditions." Proc. Natl. Acad. Sci. 2014 Jan 7; 111(1): 219-24.