title: Anomalous diffusion of oligomerized transmembrane proteins.
abstract: Transmembrane proteins frequently form (transient) oligomers on biomembranes, e.g., while participating in protein sorting and signaling events. Using coarse-grained membrane simulations we show here that transmembrane proteins show a subdiffusive motion on short time scales when being part of a linear oligomer, i.e., a flexible polymer, embedded in a two-dimensional membrane. Our results are in agreement with previous experimental observations. They further indicate that polymers of transmembrane proteins are well described by predictions from Rouse theory in two dimensions even in the presence of hydrodynamic interactions.
authors.affiliation: Laboratory for Computational Cell Biology, Department of Cell Biology, Harvard Medical School, Massachusetts 02115, USA.
authors.forename: Ulrich
authors.initials: U
authors.lastname: Schmidt
authors.forename: Matthias
authors.initials: M
authors.lastname: Weiss
mesh_terms: D001704:Biopolymers / Q000737:chemistry; D003198:Computer Simulation; D004058:Diffusion; D057446:Hydrodynamics; D008565:Membrane Proteins / Q000737:chemistry*; D008566:Membranes / Q000737:chemistry*; D008956:Models, Chemical
chemical_list: D001704:Biopolymers; D008565:Membrane Proteins