J. R. Espinosa

The paper uses a coarse-grained model to analyze how amino acid mutations affect the stability of prion-like domains across multiple proteins, revealing scaling laws that predict condensate behavior.

This study shows that the location and number of LARKS in proteins affect the viscoelastic properties and aging of biomolecular condensates, with multiple LARKS leading to gel-like behavior.

This study compares computational methods to measure viscoelasticity of biomolecular condensates in simulations, finding that SSRMI and OS techniques outperform BT in efficiency and accuracy.

This study uses simulations to show how RNA length and concentration affect RNA-protein condensate stability through distinct mechanisms involving surfactant-like and core-saturation roles of different RNA lengths.

The paper shows that FUS condensates during aging exhibit solid/liquid coexistence, with the transition initiated at the interface between dense and dilute phases.

The paper shows that inter-protein β-sheets increase RNA-binding protein condensate viscosity and alter network connectivity, leading to gelation, but RNA can slow this process.

This study shows HMGA1a undergoes phase separation in the nucleus, driven by protein-DNA interactions and its disordered C-terminal tail.

This study develops a coarse-grained model to investigate how changes in protein interaction strength during condensate maturation affect their shape and solid-like properties over time.

This study investigates how RNA length affects the stability of RNA-binding protein condensates through computational simulations of homotypic and heterotypic interactions.

The paper shows that size-conserved biomolecular condensates can form spontaneously through phase separation of scaffolds and surfactant clients, depending on their concentration ratios.

This study uses a coarse-grained model to show RNA modulates phase-separated condensate stability and transport properties through dual mechanisms depending on RNA concentration and length.

The paper shows that proteins forming liquid condensates can reenter a phase-separated state at high salt concentrations due to hydrophobic and non-ionic interactions, distinct from low-salt electrostatic-driven phase separation.

The paper investigates how surface electrostatics influence the stability of biomolecular condensates by comparing their fusion propensity using zeta potential measurements and molecular modeling.

This study shows oligonucleotides enhance liquid-liquid phase separation by acting as superscaffolds, increasing molecular connectivity and reducing barriers for phase separation in protein-oligonucleotide mixtures.