Phase separation of intrinsically disordered proteins is important for the formation of membraneless organelles or biomolecular condensates, which play key roles in the regulation of biochemical processes within cells. In this work, we investigated the phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins and discovered a surprisingly rich phase behavior. We studied both the fraction of total hydrophobic parts and the distribution of hydrophobic parts. Not surprisingly, sequences with larger hydrophobic fractions showed conventional liquid–liquid phase separation. The location of the critical point was systematically influenced by the terminal beads of the sequence due to changes in interfacial composition and tension. For sequences with lower hydrophobicity, we observed not only conventional liquid–liquid phase separation but also re-entrant phase behavior in which the liquid phase density decreases at lower temperatures. For some sequences, we observed the formation of open phases consisting of aggregates, rather than a normal liquid. These aggregates had overall lower densities than the conventional liquid phases and exhibited complex geometries with large interconnected string-like or membrane-like clusters. Our findings suggest that minor alterations in the ordering of residues may lead to large changes in the phase behavior of the protein, a fact of significant potential relevance for biology.

Phase separation of intrinsically disordered proteins is important for the formation of membraneless organelles, or biomolecular condensates, which play key roles in the regulation of biochemical processes within cells. In this work, we investigated the phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins and discovered a surprisingly rich phase behavior. We studied both the fraction of total hydrophobic parts and the distribution of hydrophobic parts. Not surprisingly, sequences with larger hydrophobic fractions showed conventional liquid-liquid phase separation. The location of the critical point was systematically influenced by the terminal beads of the sequence, due to changes in interfacial composition and tension. For sequences with lower hydrophobicity, we observed not only conventional liquid-liquid phase separation, but also reentrant phase behavior, in which the liquid phase density decreases at lower temperatures. For some sequences, we observed formation of open phases consisting of aggregates, rather than a normal liquid. These aggregates had overall lower densities than the conventional liquid phases, and exhibited complex geometries with large interconnected string-like or membrane-like clusters. Our findings suggest that minor alterations in the ordering of residues may lead to large changes in the phase behavior of the protein, a fact of significant potential relevance for biology.

Many animals perceive odorant molecules by collecting information from ensembles of olfactory neurons. These neurons employ receptors that are tuned to recognize odorant molecules by chemical binding affinity. Olfactory systems are able, in principle, to detect and discriminate large numbers of odorants by using combinatorial coding strategies. Multineuronal imaging, combined with high-throughput stimulus delivery, allow for the comprehensive measurement of ensemble-level sensory representations. Here, we used microfluidics and multineuronal imaging to study olfactory representations at the sensory periphery of the nematode C. elegans. The collective activity of chemosensory neurons in C. elegans reveals high-dimensional representations of olfactory information across a broad space of odorant molecules. We reveal diverse tuning properties and dose-response curves across chemosensory neurons and across odorant molecules. We describe the unique contribution of each sensory neuron to an ensemble-level olfactory code, and show how the encoding of a set of natural stimuli, nematode pheromones, differs from the encoding of small volatile organic molecules. The integrated activity of the sensory periphery of C. elegans contains sufficient information to robustly encode the intensity and identity of a broad panel of odorants.

We study the robustness of the paradigmatic Resonating Valence Bond (RVB) spin liquid and its orthogonal version, the quantum dimer model, on the kagome lattice. The non-orthogonality of singlets in the RVB model and the induced finite length scale not only makes it difficult to analyze, but can also significantly affect its physics, such as its resilience to perturbations. Surprisingly, we find that this is not the case: The robustness of the RVB spin liquid is not affected by the finite correlation length, which demonstrates that the dimer model forms a viable model for studying RVB physics under perturbations. A microscopic analysis, based on tensor networks, allows us to trace this robustness back to two universal mechanisms: First, the dominant correlations in the RVB are spinon correlations, making the state robust against doping with visons. Second, reflection symmetry stabilizes the spin liquid against doping with spinons, by forbidding mixing of the initially dominant correlations with the correlations which lead to the breakdown of topological order. arXiv:1910.06355v1 [cond-mat.str-el]