The research focus in my lab is on complex integral membrane proteins and in particular ion channels and transporters. We engage a multidisciplinary aproach using a combination of advanced biophysical and biochemical methods spanning from x-ray crystallography and pulsed-EPR to analytical mass and single molecule methodologies to investigate the gating mechanism of these important and challenging systems.
X-ray hanging drop and lipidic cubic phase crystallography is used to obtain structural information to molecular detail and solve membrane protein structures in distinct conformational states. Our aim is to elucidate ion channel gating mechanisms and understand through the use of model systems the fundamental biophysical property of mechanosensation.
X-ray structures represent snapshots frozen in time and dynamic information is required to monitor conformational rearrangements during gating. Pulsed-electron-electron double resonance (PELDOR) spectroscopy, also known as DEER, is used in combination with site-directed spin labeling (SDSL) to obtain structural information (i.e. spin-to-spin distances within the complex).
Mass spectrometry is used to identify potential substrates and characterise their interaction with the macromolecule of interest, while the effect on protein function is monitored using single molecule methodologies, in order to create a valid link between structure and function.
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