Functional state modulation of membrane proteins by dynamic association and dissociation (A03)

• Subject Area: Biophysics
• Term: since 2016
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 267205415

We intend to investigate how dynamic association and dissociation modulate the functional state of membrane proteins. We will address this question on two systems, I) molecular components central for ethylene perception in plants, and II) PlaF, a phospholipase A from P. aeruginosa suggested to be a viru-lence factor. By molecular simulations and modeling in close connection with experiments, we will generate structural models of receptor/chaperone complexes to scrutinize the mechanism of copper transfer to ETR1, investigate structural dynamics of apo and ethylene-bound ETR1, and scrutinize the molecular mechanism underlying PlaF inhibition by fatty acids and the role of PlaF/protein interactions for regulation of PlaF function.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 1208: Identity and Dynamics of Membrane Systems - from Molecules to Cellular Functions
• Applicant Institution: Heinrich-Heine-Universität Düsseldorf
• Project Head: Professor Dr. Holger Gohlke