Fleurie M. Kelley

TL;DR: This work explores a model protein, the disordered N-terminal domain of LAF-1, and highlights how three key features of the sequence control the protein’s propensity to phase-separate, and identifies a region of the RGG domain that has high contact probability and is highly conserved between species; deletion of this region significantly disrupts phase separation in vitro and in vivo.

TL;DR: A model protein, the disordered N-terminal domain of LAF-1, is explored, and it is found that phase behavior of this model IDP is dictated by the presence of a short conserved domain, charge patterning, and arginine-tyrosine interactions.

TL;DR: A micropipette-based technique is developed that uniquely, to the knowledge, allows quantifications of both the surface tension and viscosity of biomolecular condensates, independent of labeling and surface-wetting effects.

TL;DR: In this article, a bio-inspired approach was used to discover how amphiphilic, surfactant-like proteins may contribute to the structure and size regulation of biomolecular condensates.

TL;DR: In this article, a micropipette-based technique was developed for quantification of both surface tension and viscosity of biomolecular condensates, independent of labeling and surface wetting effects.