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Helena Casademunt

Researcher at Princeton University

Publications -  5
Citations -  198

Helena Casademunt is an academic researcher from Princeton University. The author has contributed to research in topics: Intrinsically disordered proteins & Phase (matter). The author has an hindex of 3, co-authored 4 publications receiving 87 citations. Previous affiliations of Helena Casademunt include Harvard University.

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Model for disordered proteins with strongly sequence-dependent liquid phase behavior

TL;DR: In this paper, the authors investigated the phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins and discovered a surprisingly rich phase behavior, including the formation of open phases consisting of aggregates, rather than a normal liquid.
Journal ArticleDOI

Model for disordered proteins with strongly sequence-dependent liquid phase behavior

TL;DR: The phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins is investigated and it is suggested that minor alterations in the ordering of residues may lead to large changes in the phase behavior of the protein.
Journal ArticleDOI

Functional imaging and quantification of multineuronal olfactory responses in C. elegans

TL;DR: 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, and describes the unique contribution of each sensory neuron to an ensemble-level olfactory code.
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Topological spin liquids: Robustness under perturbations

TL;DR: In this article, the robustness of the kagome resonating valence bond (RVB) spin liquid and its orthogonal version, the quantum dimer model, was studied.
Posted ContentDOI

Model for disordered proteins with strongly sequence-dependent liquid phase behavior

TL;DR: The phase separation of different sequences of a coarse-grained model for intrinsically disordered proteins is investigated and a surprisingly rich phase behavior is discovered, suggesting that minor alterations in the ordering of residues may lead to large changes in the phase behavior of the protein.