Abstract
Intrinsically disordered proteins undergo liquid-liquid phase separation to form biological condensates that play essential roles in a variety of cellular processes, including chromatin organization. Computational approaches can give unique insight into the molecular structures of such condensates; however, predicting the interplay between multiple proteins, which may have both ordered and disordered domains, remains challenging. To move toward a unified coarse-grained force field for ordered and disordered proteins, we developed the maximum entropy optimized force field, which can predict the radius of gyration of ordered and disordered proteins, while ensuring the folded structures of ordered proteins are lower in energy than other states.
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