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

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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.