Issue 2, 2019

Effect of protein–protein interactions and solvent viscosity on the rotational diffusion of proteins in crowded environments

Abstract

The rotational diffusion of a protein in the presence of protein crowder molecules was analyzed via computer simulations. Cluster formation as a result of transient intermolecular contacts was identified as the dominant effect for reduced rotational diffusion upon crowding. The slow-down in diffusion was primarily correlated with direct protein–protein contacts rather than indirect interactions via shared hydration layers. But increased solvent viscosity due to crowding contributed to a lesser extent. Key protein–protein contacts correlated with a slow-down in diffusion involve largely interactions between charged and polar groups suggesting that the surface composition of a given protein and the resulting propensity for forming interactions with surrounding proteins in a crowded cellular environment may be the major determinant of its diffusive properties.

Graphical abstract: Effect of protein–protein interactions and solvent viscosity on the rotational diffusion of proteins in crowded environments

Article information

Article type
Paper
Submitted
01 Oct 2018
Accepted
11 Dec 2018
First published
12 Dec 2018

Phys. Chem. Chem. Phys., 2019,21, 876-883

Author version available

Effect of protein–protein interactions and solvent viscosity on the rotational diffusion of proteins in crowded environments

G. Nawrocki, A. Karaboga, Y. Sugita and M. Feig, Phys. Chem. Chem. Phys., 2019, 21, 876 DOI: 10.1039/C8CP06142D

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