Protein–lipid interactions
Quantify lipid binding, selectivity, stoichiometry, competition, and cooperativity at the level of intact membrane protein complexes.
Research
Membrane chemistry controls protein function.
Biological membranes are chemically complex, dynamic environments. We develop and apply native mass spectrometry, structural biology, biophysics, and protein engineering to determine how lipids, metal ions, and other molecular partners regulate membrane proteins.
A unique interfaceOur work connects molecular measurements in native-like membrane environments with structural and functional mechanisms.
Native MSCryo-EMLipidomicsBiophysics
01 · Molecular recognition
Membrane chemistry
Membrane proteins interact with a chemically diverse lipid environment rather than an inert solvent. We ask which lipids are selectively recognized, how acyl-chain and headgroup chemistry influence binding, and how these interactions propagate into changes in protein structure and function.
Metals and cofactors
Define how metal ions and other chemical inputs reshape lipid recognition and alter membrane-protein assemblies.
02 · Force sensing
Mechanosensation & ion channels
We investigate how membrane composition, lipids, and metal ions tune the conformational landscape and pressure sensitivity of K2P channels, while related studies probe chemical regulation of Kir channels.
TRAAK, TREK1 & TREK2
Connect defined membrane chemistry to lipid occupancy, conformational changes, and the molecular mechanisms of force sensing and gating.
PIP2, metals & cooperativity
Investigate how chemical inputs modulate lipid binding and cooperative regulation in inwardly rectifying potassium channels.
03 · Technology
Native mass spectrometry
Native MS preserves noncovalent interactions and provides direct access to intact molecular assemblies. The laboratory develops methods that extend these measurements to increasingly native-like membrane environments and to processes that have traditionally been difficult to quantify.
Thermodynamics
Resolve individual lipid-binding events and quantify how membrane chemistry shapes molecular recognition.
Kinetics
Use time-resolved native MS to directly measure biomolecular association and reaction kinetics.
Native-like membranes
Study intact complexes in detergents, proteoliposomes, nanodiscs, and saposin-based nanoparticles.
Instrumentation
Develop charge manipulation, direct mass, ion-mobility, and complementary strategies for challenging assemblies.
04 · Mechanism
Structure & function
Mass spectrometry reveals what is bound and how strongly; structural and functional measurements reveal why it matters. We combine cryo-EM, crystallography, mutagenesis, and biochemical or cellular assays to connect molecular interactions to mechanism.
Defined membrane environments
Determine structures in controlled lipid compositions to visualize conserved and lipid-dependent conformational states.
Structure-guided experiments
Test mechanistic hypotheses using mutations, functional measurements, and complementary biochemical approaches.
Biological systems
From channels to signaling
The laboratory works across membrane proteins and membrane-associated signaling assemblies, using systems that expose different aspects of molecular recognition and regulation.
K2P channels
Mechanosensation, lipid modulation, metal-dependent regulation, and membrane-coupled gating.
Kir channels
PIP2 recognition, metal coordination, and cooperative lipid binding.
ABC transporters
Membrane-protein lipid interactions, cofactors, conformational regulation, and transport mechanisms.
RAS signaling
Membrane-dependent assembly of oncogenic signaling proteins and the chemistry controlling their interactions.
See the work behind these questions.
Browse the lab’s full publication record, including recent work in native MS, membrane-protein chemistry, and structural biology.