Michael Marty

Michael Marty is an Associate Professor of chemistry at The University of Texas at Austin. Marty earned his B.A. in chemistry and mathematics at St. Olaf College. He then completed his Ph.D. in chemistry as a Springborn Fellow at the University of Illinois Urbana-Champaign with Prof. Stephen Sligar and went on to postdoctoral research at the University of Oxford with Prof. Dame Carol Robinson. He joined the faculty at The University of Arizona in 2016 and moved to The University of Texas in 2025. His research applies lipoprotein nanodiscs with mass spectrometry to study membrane proteins and their interactions with lipid bilayers. 

Membrane proteins play critical biochemical roles and constitute the majority of drug targets. Despite their importance, they remain challenging to study because of their amphipathic nature and low expression levels. In addition, the lipid bilayer plays an important but still poorly understood role in regulating membrane protein structure and function. New analytical and biochemical methods are needed to better understand membrane proteins and support the development of drugs that target them.

The Marty lab develops mass spectrometry methods to study the structure and biophysics of membrane proteins. Working at the interface of analytical chemistry and biochemistry, the group uses lipoprotein nanodiscs to solubilize membrane proteins in lipid bilayers with defined compositions. Nanodiscs are nanoscale discoidal lipid bilayers encircled by two amphipathic membrane scaffold proteins.

Using nondenaturing nano-electrospray ionization, the group preserves intact nanodisc complexes within the mass spectrometer and gradually releases membrane proteins through collisional activation. This approach, known as native mass spectrometry, enables measurement of the stoichiometry and lipid composition of large protein-lipid complexes and provides insight into protein-lipid interactions in membrane receptors and transporters.

Because mass spectra of nanodiscs are highly complex, the group develops computational approaches and software for the analysis of native mass spectrometry data. This work builds on UniDec, software developed by the laboratory to rapidly and robustly deconvolve mass spectra.

The group also develops lipidomics experiments to measure lipid binding affinities to membrane proteins. Using LC-MS/MS, researchers identify and quantify lipids in nanodiscs with and without membrane proteins, examining the enrichment of specific lipids associated with particular membrane protein targets. These studies leverage advanced lipidomics techniques to better understand membrane protein function.