Structural and dynamical studies of ß-strand-membrane proteins by liquid-/solid-state NMR spectroscopy (A04)

• Subject Area: Structural Biology
• Term: from 2009 to 2020
• Project identifier: Deutsche Forschungsgemeinschaft (DFG) - Project number 55908123

After the successful structure determination of the open state of the channel protein hVDAC1, we now aim at determining the high resolution structure of the closed state by using a quintuple VDAC1 mutant that electrophysiologically behaves like a closed state of hVDAC1. Furthermore, we will study the structure of Aß and IAPP oligomers in membranes with and without the oligomer modulator anle138b. Both Aß and IAPP oligomers induce ion conductivity and are related to neuronal (Alzheimer) as well as ß-cell dysfunction and death (type II diabetes), which is rescued in mouse models by anle138b.

• DFG Programme: Collaborative Research Centres
• Subproject of: SFB 803: Functionality Controlled by Organisation in and between Membranes
• Applicant Institution: Georg-August-Universität Göttingen
• Project Heads: Dr. Loren Andreas, since 1/2017; Professor Dr. Christian Griesinger; Professor Dr. Adam Lange, until 3/2014; Professor Rasmus Linser, Ph.D., from 10/2014 until 12/2016