Crowding in cellular environments results in constant non-specific interactions between macromolecules impacting their stability and dynamics. Past studies have indicated that diffusion is retarded significantly upon crowding but the details of how the slow-down in diffusion depends on protein-protein interactions is not as clear. Analysis of computer simulations of crowded protein solutions ranging from homogeneous solutions of small model proteins such as villin to large cytoplasmic models is presented and compared to experimental data from NMR spectroscopy. The results offer new insights into transient weak associations of proteins under crowded conditions that is reflected in reduced translational and rotational diffusion rates. The simulations also offer an opportunity to critically evaluate the ability of current force fields to accurately capture the interactions of proteins under realistic cellular conditions.<br/>

Diffusional dynamics of proteins under crowded conditions

254th National Meeting (2017)

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