(607f) A Coarse-Grained Model to Elucidate the Regulation of Protein Phase Behavior By Post Translational Modifications
Here, we expand upon our amino acid resolution coarse-grained model to represent the biomolecular interactions exerted among non-canonical, and post-translationally modified amino acids in order to investigate how the position and the number of post-translationally modified sites can alter the phase behavior of proteins. To do so, we use a slab-geometry molecular dynamics method to calculate the phase diagram . We investigate the most-frequently occurring post-translational modifications seen in the modulation of LLPS, including phosphorylation, methylation, acetylation and ubiquitination. Being in agreement with experimental observations, our model is able to capture that arginine dimethylation of hnRNPA2 protein decreases the phase separation whereas tyrosine phosphorylation causes a drop in the critical temperature, thus enhancing phase separation.
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