In view of the notorious complexity of protein--protein interactions, simplified models of proteins treated as patchy particles offer a promising strategy to obtain insight into the mechanism of crystallization. Here we report liquid--liquid phase separation (LLPS) with a highly asymmetric coexistence region in a computational model of rubredoxin with real molecular shape. The coexistence region terminates in both an upper (UCST) and a lower (LCST) critical solution temperature, and the complex molecular shape explains the closed-loop behavior of the LLPS.
@article{arxiv.1910.06865,
title = {Looped liquid-liquid coexistence in protein crystallization},
author = {Jens Glaser and Sharon C. Glotzer},
journal= {arXiv preprint arXiv:1910.06865},
year = {2019}
}