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Intrinsically disordered proteins (IDPs) are important for biologicalfunctions. In contrast to folded proteins, molecular recognition among certainIDPs is "fuzzy" in that their binding and/or phase separation arestochastically governed by the interacting IDPs' amino acid sequences whiletheir assembled conformations remain largely disordered. To help elucidate abasic aspect of this fascinating yet poorly understood phenomenon, the bindingof a homo- or hetero-dimeric pair of polyampholytic IDPs is modeled statisticalmechanically using cluster expansion. We find that the binding affinities ofbinary fuzzy complexes in the model correlate strongly with a newly derivedsimple "jSCD" parameter readily calculable from the pair of IDPs' sequencecharge patterns. Predictions by our analytical theory are in essentialagreement with coarse-grained explicit-chain simulations. This computationallyefficient theoretical framework is expected to be broadly applicable torationalizing and predicting sequence-specific IDP-IDP polyelectrostaticinteractions.

Analytical Theory for Sequence-Specific Binary Fuzzy Complexes of Charged Intrinsically Disordered Proteins