One research axis concerns membrane binding proteins containing short membrane anchors, that confer nanodomain formation, i.e. dynamic lipid and protein clustering in the membrane, such as the plant protein remorin. For these proteins, the analysis of structures and interactions remains a challenge because of their intrinsic dynamic nature and the subtle interactions that guide protein condensation and nanodomain formation on the membrane. Solid-state NMR is a powerful tool to obtain information on these complex systems at an atomic scale and perfectly suited to complement bioinformatics and diverse experimental approaches. The example of the plant protein remorin explicits well the challenges that arise from peripheral membrane-binding protein structures. As for now, we could show that Solanum tuberosum remorins bind

preferentially to phosphatidylinositolphosphates (PIPs) over the C-terminal membrane anchor and they confer nanodomain clustering over their lipid membrane binding characteristics, coiled-coil oligomerization behaviour and phosphorylation status of the intrinsically disordered domain. However, many questions to define family-dependent structural determinants, nanodomain clustering characteristics and remorin's potential to oligomerize and condensate remain unsolved. 

 

Another major research axis concerns protein assemblies such as found in amyloid aggregates or molecular machines. Amyloids are a intriguing protein species that can either contribute to detrimental cellular disfunctioning such as in (neuro-)degenerative diseases or play essential functional roles, relying on their potential to assemble into highly stable amyloids. The characteristics of amyloids reside in the underlying molecular beta-strand arrangement that results in unbranched filaments with several nanometer width and undefined length. A favorable beta-sheet assembly approximately perpendicular to the filament axis can further stabilise the fibers. In line with the versatile and stable resulting structure, these molecular objects provide specific templating mechanisms as we have shown for the amyloid prion HELLF, involved in cell death signalling in the filamentous fungus Podospora anserina. For instance, using mainly solid-state NMR, we have demonstrated its capacity of sequence-selectively templating its beta solenoid amyloid structure without respecting structural similarities imposed by structurally equivalent templates.