Most proteins are post-translationally modified (PTM) inside cells. This means that endogenous cellular enzymes covalently alter the chemical properties of individual protein residues. They do so in a highly dynamic and reversible manner.
We employ in-cell NMR spectroscopy to directly analyze how these PTMs affect protein structure and function in different cellular environments.
Because in-cell NMR spectroscopy is a non-invasive and non-destructive analytical tool we study cellular PTMs in a continuous, time-resolved and quantitative fashion.
This allows us to investigate dynamic changes of cellular PTM states in response to different signaling events.
We are further developing new NMR methods to detect different cellular PTMs by in-cell NMR spectroscopy.
While protein phosphorylation and acetylation are of particular interest to us, we are also targeting cellular methylation, oxidation and proteolytic processing events.