@article{larsen_rosholm_kennard_pedersen_munch_tkach_sakon_bjornholm_weninger_bendix_et al._2020, title={How Membrane Geometry Regulates Protein Sorting Independently of Mean Curvature}, volume={6}, ISSN={["2374-7951"]}, DOI={10.1021/acscentsci.0c00419}, abstractNote={Biological membranes have distinct geometries that confer specific functions. However, the molecular mechanisms underlying the phenomenological geometry/function correlations remain elusive. We studied the effect of membrane geometry on the localization of membrane-bound proteins. Quantitative comparative experiments between the two most abundant cellular membrane geometries, spherical and cylindrical, revealed that geometry regulates the spatial segregation of proteins. The measured geometry-driven segregation reached 50-fold for membranes of the same mean curvature, demonstrating a crucial and hitherto unaccounted contribution by Gaussian curvature. Molecular-field theory calculations elucidated the underlying physical and molecular mechanisms. Our results reveal that distinct membrane geometries have specific physicochemical properties and thus establish a ubiquitous mechanistic foundation for unravelling the conserved correlations between biological function and membrane polymorphism.}, number={7}, journal={ACS CENTRAL SCIENCE}, author={Larsen, Jannik B. and Rosholm, Kadla R. and Kennard, Celeste and Pedersen, Soren L. and Munch, Henrik K. and Tkach, Vadym and Sakon, John J. and Bjornholm, Thomas and Weninger, Keith R. and Bendix, Poul Martin and et al.}, year={2020}, month={Jul}, pages={1159–1168} } @article{lim_karpusenko_sakon_hook_lamar_riehn_2011, title={DNA methylation profiling in nanochannels}, volume={5}, number={3}, journal={Biomicrofluidics}, author={Lim, S. F. and Karpusenko, A. and Sakon, J. J. and Hook, J. A. and Lamar, T. A. and Riehn, R.}, year={2011} } @article{sakon_weninger_2010, title={Detecting the conformation of individual proteins in live cells}, volume={7}, ISSN={["1548-7105"]}, DOI={10.1038/nmeth.1421}, abstractNote={We combined single-molecule fluorescence resonance energy transfer (smFRET) with single-particle tracking in live cells to detect the in vivo conformation of individual proteins. We site-specifically labeled recombinant SNARE proteins with a FRET donor and acceptor before microinjecting them into cultured cells. Individual proteins rapidly incorporated into folded complexes at the cell membrane, demonstrating the potential of this method to reveal dynamic interactions within cells.}, number={3}, journal={NATURE METHODS}, author={Sakon, John J. and Weninger, Keith R.}, year={2010}, month={Mar}, pages={203–U56} }