Francesca M. Marassi

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 study identifies a hydrophobic groove on vitronectin's HX domain that binds phospholipids and mediates its association with HDL through structural modeling and simulations.

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.

This paper introduces an in-silico method using Feret signatures to characterize nanodisc samples, enabling the identification of low-heterogeneity preparations for accurate structure determination of membrane proteins.