We are chemists, biochemists, structural biologists, and mass spectrometrists working together to understand how membrane chemistry controls protein structure, interactions, and function.
The Laganowsky Lab investigates how the chemical environment of biological membranes regulates membrane protein structure, interactions, and function, combining native mass spectrometry with structural, biochemical, and biophysical approaches.
I develop mass spectrometry approaches for measuring protein–ligand binding kinetics and dissecting endogenous protein complexes to reveal their composition, proteoform heterogeneity, and molecular interactions.
I apply Salipro nanodisc technology and native mass spectrometry to investigate membrane protein–lipid interactions.
Investigating how lipids and other cofactors regulate potassium ion channel activity.
Developing time-resolved native mass spectrometry to directly measure the kinetics of biomolecular interactions.
Examining how lipids regulate the activity of the lipid flippase MsbA to better understand lipid-dependent control of bacterial outer-membrane assembly.
