About 30 % of volume fraction in the cytoplasm is occupied by macromolecules, like proteins or nucleic acids. This environment is often called as 'macromolecular crowding' and is considered to affect conformational stability, dynamics and functions of proteins in the cytoplasm. However, due to the experimental limitation, it is still difficult to measure molecular properties under macromolecular crowding environment. Here, we carry out explicit solvent molecular dynamics simulations of a series of protein-G and protein-G/villin mixed systems at different protein concentrations to investigate hydration structure and dynamics. The self-diffusion rates and dielectric constants for water are drastically changed as a function of crowding. This information can be useful for modeling larger fraction of the cytoplasm using computer simulations based on the all-atom or coarse-grained models.

Hydration structure and dynamics under protein crowding environments

244th National Meeting (2012)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.