Tuesday, 26 June 2007 - 12:00 PM
Pencader 117
200

Brownian and colloidal interactions in protein crystal growth

Jack Lum, Johns Hopkins University, Laurel, MD

Brownian dynamic simulations are used to elucidate some of the underlying transport processes of protein molecules in protein crystallization. The dominant forces are modeled from colloidal interactions between a lysozyme molecule (sphere) and tetragonal lysozyme crystal (wall), both heterogeneously charged. The electrostatic portion is obtained by solving the linearized Poisson-Boltzmann equation with a boundary elements method; the van der Waals force is treated as a function of only the Hamaker constant and sphere-wall separation. Simulation results show that protein molecules have greater translational diffusivity and are more concentrated near a highly charged crystal surface than near a weakly charged one. This suggests that ordered protein assembly as a precursor to crystal growth is more likely to occur at the crystal surface than in bulk solution.