Protein Interactions in Solution Characterized by Light and Neutron Scattering: Comparison of Lysozyme and Chymotrypsinogen

摘要: The effects of pH and electrolyte concentration on protein-protein interactions in lysozyme chymotrypsinogen solutions were investigated by static light scattering (SLS) small-angle neutron (SANS). Very good agreement between the values virial coefficients measured SLS SANS was obtained without use adjustable parameters. At low concentration, depend strongly change from positive to negative as increases. All at high salt are slightly weakly pH. For lysozyme, always decrease with increasing concentration. However, for there is a cross-over point around 5.2, above which ionic strength, indicating presence attractive electrostatic interactions. data Derjaguin-Landau-Verwey-Overbeek (DLVO)-type modeling, accounting repulsive electrostatic, van der Waals, excluded volume equivalent colloid spheres. This model, however, unable resolve complex short-ranged orientational results protein precipitation crystallization experiments qualitative correlation patterns demonstrate that interaction mapping could help outline new regions.