Rotational Diffusion of Membrane Proteins in Crowded Membranes
| Autor: | O. H. Samuli Ollila, Matti Javanainen, Hector Martinez-Seara |
|---|---|
| Přispěvatelé: | Biophysical chemistry, Institute of Biotechnology |
| Rok vydání: | 2020 |
| Předmět: |
DYNAMICS
Membranes Chemistry LIPID-MEMBRANES Protein dynamics Cell Membrane Dynamics (mechanics) Membrane Proteins Rotational diffusion RHODOPSIN Molecular Dynamics Simulation BROWNIAN-MOTION Surfaces Coatings and Films Diffusion Molecular dynamics Transmembrane domain Membrane Membrane protein FORCE-FIELD Materials Chemistry Biophysics 1182 Biochemistry cell and molecular biology ORIENTATION Physical and Theoretical Chemistry Brownian motion |
| Zdroj: | The Journal of Physical Chemistry B. 124:2994-3001 |
| ISSN: | 1520-5207 1520-6106 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|