Membrane proteins travel along cellular membranes and reorient themselves to form functional oligomers and protein-lipid complexes. Following the Saffman-Delbrück model, protein radius sets the rate of this diffusive motion. However, it is unclear how this model, derived for ideal and dilute membranes, performs under crowded conditions of cellular membranes. Here, we study the rotational motion of membrane proteins using molecular dynamics simulations of coarse-grained membranes and 2-dimensional Lennard-Jones fluids with varying levels of crowding. We find that the Saffman-Delbrück model captures the size-dependency of rotational diffusion under dilute conditions where protein-protein interactions are negligible, whereas stronger scaling laws arise under crowding. Together with our recent work on lateral diffusion, our results reshape the description of protein dynamics in native membrane environments: The translational and rotational motions of proteins with small transmembrane domains are rapid, whereas larger proteins or protein complexes display substantially slower dynamics.

Computational Physics Laboratory Tampere University Tampere 33720 Finland

Institute of Biotechnology University of Helsinki Helsinki 00014 Finland

Institute of Organic Chemistry and Biochemistry Czech Academy of Sciences Prague 166 10 Czech Republic

References provided by Crossref.org

Protein Crowding and Cholesterol Increase Cell Membrane Viscosity in a Temperature Dependent Manner