Assembly and Electrostatic Steering of α-lactalbumin/ Lysozyme Heterodimers: Kirkwood Correlation

The interaction of LYS with native α-LA (holo α-LA) and its calcium-depleted form (apo α- LA) is investigated using Dielectric Relaxation Spectroscopy (DRS) and Dynamic Light Scattering (DLS). Here, the interaction between LYS and α-LA change the diffusion coefficient of substrate and newly formed oligomer exhibit its characteristic Brownian motion, as followed by DLS. We report on our efforts towards the understanding of the interaction occurring between these two proteins. To describe the possible, assemble in more detail, protein-protein docking simulations was provided. In a docking simulation, several putative structural models of heterodimers are selected by scoring functions from an ensemble of many heterodimer models. The low docking score of these models was used to obtain theoretical values of the dipole moment and hydrodynamic radius using PHEMTO Server and HYDROPRO program, respectively