Honors & Awards


  • Postdoctoral Fellowship (Nurturing Next-Generation Researchers), National Research Foundation of Korea (2021 - 2024)

Professional Education


  • Doctor of Philosophy, Korea Advanced Institute of Science and Technology (KAIST), Chemistry (2021)
  • Bachelor of Science, Korea Advanced Institute of Science and Technology (KAIST), Chemistry (2015)

Stanford Advisors


All Publications


  • Behavior control of membrane-less protein liquid condensates with metal ion-induced phase separation NATURE COMMUNICATIONS Hong, K., Song, D., Jung, Y. 2020; 11 (1): 5554

    Abstract

    Phase separation of specific biomolecules into liquid droplet-like condensates is a key mechanism to form membrane-less organelles, which spatio-temporally organize diverse biochemical processes in cells. To investigate the working principles of these biomolecular condensates as dynamic reaction centers, precise control of diverse condensate properties is essential. Here, we design a strategy for metal ion-induced clustering of minimal protein modules to produce liquid protein condensates, the properties of which can be widely varied by simple manipulation of the protein clustering systems. The droplet forming-minimal module contains only a single receptor protein and a binding ligand peptide with a hexahistidine tag for divalent metal ion-mediated clustering. A wide range of protein condensate properties such as droplet forming tendency, droplet morphology, inside protein diffusivity, protein recruitment, and droplet density can be varied by adjusting the nature of receptor/ligand pairs or used metal ions, metal/protein ratios, incubation time, binding motif variation on recruited proteins, and even spacing between receptor/ligand pairs and the hexahistidine tag. We also demonstrate metal-ion-induced protein phase separation in cells. The present phase separation strategy provides highly versatile protein condensates, which will greatly facilitate investigation of molecular and structural codes of droplet-forming proteins and the monitoring of biomolecular behaviors inside diverse protein condensates.

    View details for DOI 10.1038/s41467-020-19391-8

    View details for Web of Science ID 000591843300009

    View details for PubMedID 33144560

    View details for PubMedCentralID PMC7642319