A. Kraft

This paper uses solid-state NMR to analyze the structure and activity of outer membrane proteins in native bacterial vesicles, showing their functionality and interactions with host ligands.

This paper identifies a pH-sensing motif in PagC, an outer membrane protein, that drives bacterial vesicle production and aggregation at acidic pH using in situ NMR and EM.

This paper introduces a Hadamard encoding method for multi-dimensional solid-state NMR spectral editing of protein sidechains, enabling unambiguous detection of signals from basic amino acids and their bound water molecules.