Rotational Diffusion of Membrane Proteins in Crowded Membranes

0524096 - ÚOCHB 2021 RIV US eng J - Článek v odborném periodiku
Javanainen, Matti - Ollila, O. H. S. - Martinez-Seara, Hector
Rotational Diffusion of Membrane Proteins in Crowded Membranes.
Journal of Physical Chemistry B. Roč. 124, č. 15 (2020), s. 2994-3001. ISSN 1520-6106. E-ISSN 1520-5207
Grant CEP: GA ČR(CZ) GX19-26854X
Institucionální podpora: RVO:61388963
Klíčová slova: lipid membranes * Brownian motion * force field
Obor OECD: Physical chemistry
Impakt faktor: 2.991, rok: 2020
Způsob publikování: Omezený přístup
https://pubs.acs.org/doi/10.1021/acs.jpcb.0c00884

Membrane proteins travel along cellular membranes and reorient themselves to form functional oligomers and proteinlipid complexes. Following the Saffman-Delbruck 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-Delbruck 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.
Trvalý link: http://hdl.handle.net/11104/0308436