Anisotropy of the Coulomb interaction between folded proteins: consequences for mesoscopic aggregation of lysozyme.

ABSTRACT: Toward quantitative description of protein aggregation, we develop a computationally efficient method to evaluate the potential of mean force between two folded protein molecules that allows for complete sampling of their mutual orientation. Our model is valid at moderate ionic strengths and accounts for the actual charge distribution on the surface of the molecules, the dielectric discontinuity at the protein-solvent interface, and the possibility of protonation or deprotonation of surface residues induced by the electric field due to the other protein molecule. We apply the model to the protein lysozyme, whose solutions exhibit both mesoscopic clusters of protein-rich liquid and liquid-liquid separation; the former requires that protein form complexes with typical lifetimes of approximat

SUBMITTER: Chan HY 

PROVIDER: S-EPMC3328725 | biostudies-literature | 2012 Apr

REPOSITORIES: biostudies-literature