Kvido Stříšovský, Jana Humpolíčková, Jan Škerle, and colleagues from IOCB Prague combined the Förster resonance energy transfer measurements and Monte Carlo simulations to determine the dimerization of membrane proteins.
Because the membrane proteins lack the freedom of rotations and the membrane is anisotropic by definition, they proposed the apparent Förster radius as a comparative quantity instead of its variant usable in solution.
Using this approach, the researchers determined that the human rhomboid protease RHBDL2 is monomeric in the lipid membrane, unlike previously suggested.
Read the paper:
- Škerle, J.; Humpolíčková, J.; Johnson, N.; Rampírová, P.; Poláchová, E.; Fliegl, M.; Dohnálek, J.; Suchánková, A.; Jakubec, D.; Strisovsky, K. Membrane Protein Dimerization in Cell-Derived Lipid Membranes Measured by FRET with MC Simulations. Biophysical Journal 2020, 118, 1861-1875. https://doi.org/10.1016/j.bpj.2020.03.011
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