Marlène Martinho

Research Interests:

For many years, my research has focused on investigating structural transitions in proteins, including intrinsically disordered proteins (IDPs), flexible proteins, metalloproteins, and membrane proteins. My main approach combines site-directed spin labeling (SDSL) with electron paramagnetic resonance (EPR) spectroscopy. I use spin probes based on nitroxide radicals or metal centers, either endogenous or introduced into proteins. In addition to monitoring local structural changes, I use spin-spin distance measurements by pulsed EPR, in particular Double Double Electron Resonance (DEER), to characterize conformational rearrangements and protein dynamics in biological systems.

In recent years, I have sought to apply my expertise in EPR spectroscopy to understanding the dynamics and oligomerization of membrane proteins.

One of my first projects in this area focused on the bacterial transporter BmrA from Bacillus subtilis, a member of the ATP-binding cassette (ABC) transporter superfamily. Our goal was to elucidate, at the molecular level, how BmrA mediates the efflux of structurally diverse antibiotics spanning a broad range of molecular sizes.

This research established a new direction for my work, extending the application of EPR-based approaches to the study of membrane protein dynamics using SDSL-EPR, an approach that remains unique within our laboratory, and complementary to other techniques. I am also interested in developing innovative approaches that combine non-canonical amino acids with SDSL-EPR, including the design and use of custom, non-commercial spin labels to expand the range of biological systems and molecular processes that can be investigated, in vitro and in cell