Protein Aggregation and Phase Behaviour in Electric Fields


My research fields are focused on collective phase behaviors of charged DNA-viruses (fd) in both non-equilibrium (electric-field and shear-flow) and equilibrium, together with developments of novel scientific instrumentation, light scatterings and image-time correlation spectroscopy. Emergent experimental results have been provided semi-empirical theories on charged species, in particular, low-frequency driven dynamical states of charged DNA rods, field-inducedmicroscopic dynamics and critical slowing down behaviors (glass phenomena) as well the flow response of soft rod-glasses with 3d bulk pattern formations. In the equilibrium phase diagram of charged DNA-rods at low ionic strengths, the orientation kinetics of charged DNA-rods are explored by image-time correlations, which also applied to other interested materials (T4 DNA, lysozyme with antagonistic salt, cellulose nano-fibers/crystals, etc).  As ongoing research interests, the protein phase behaviors and amorphous protein aggregations in weak electric fields are to revealed by roles of dissociation constant for condensed ions in both non-equilibrium and equilibrium. To which extent can protein aggregation be inhibited/enhanced by electric fields (also in mixtures of different proteins)? The main topic is how the electric field-induced change of the electrical double layer affect on the structure of proteins (exposure of hydrophobic groups).

Research Topics

  • The effect of electric fields, shear flow, and confinement on the dynamics and self-assembly as well as field-induced instabilities of suspensions of anisotropic nano-particles.
  • Protein aggregation and phase behaviour in electric fields.


Dr. Kyongok Kang


Building 04.6 / Room 94b

+49 2461/61-6089


Protein Aggregation and Phase Behaviour in Electric Fields
(A,B) A schematic of the electric-field induced deformation of the (primary) structure of a protein due to electric forces acting on charged groups within the protein. For more “floppy” proteins the secondary structure will be most severely affected. (C) A preliminary phase diagram of lysozyme as a function of the frequency of the electric field (with a fixed field strength) and the added amount of the denaturant NaSCN. If no salt is added, protein droplets (D) form. On increasing the frequency, they transform to fibres, rings and tubes (T) that dissociate at the highest frequencies. If salt is added, crystalline (C), phase separated (L + L), and twisted nematic (TN) states occur.


Projects & Cooperations

DFG Einzelantrag “Protein phase behaviour in electric fields“, with the HHU (Dr. Florian Platten).

Last Modified: 09.01.2023