title: Protein phase behavior and crystallization: effect of glycerol.
abstract: Glycerol is widely used as an additive to stabilize proteins in aqueous solution. We have studied the effect of up to 40 wt % glycerol on the crystallization of lysozyme from brine. As the glycerol concentration increased, progressively larger amounts of salt were needed to crystallize the protein. Like previous authors, we interpret this as evidence for glycerol changing the interaction between lysozyme molecules. We quantitatively model the interprotein interaction using a Derjaguin-Landau-Verwey-Overbeek potential. We find that the effect of glycerol can be entirely accounted for by the way it modifies the dielectric constant and refractive index of the solvent. Quantifying the interprotein interaction by the second virial coefficient, B(2), we find a universal crystallization boundary for all glycerol concentrations.
authors: Scottish Universities Physics Alliance (SUPA), School of Physics, The University of Edinburgh, Mayfield Road, Edinburgh EH9 3JZ, Scotland.
authors: H
authors: H
authors: Sedgwick
authors: J E
authors: JE
authors: Cameron
authors: W C K
authors: WC
authors: Poon
authors: S U
authors: SU
authors: Egelhaaf
mesh_terms: D000818:Animals; D002021:Buffers; D002645:Chickens; D003460:Crystallization / Q000379:methods; D004305:Dose-Response Relationship, Drug; D005990:Glycerol / Q000737:chemistry*; D006851:Hydrochloric Acid / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D009113:Muramidase / Q000737:chemistry*; D011485:Protein Binding; D012492:Salts / Q000737:chemistry; D019346:Sodium Acetate / Q000737:chemistry; D012995:Solubility; D012996:Solutions / Q000737:chemistry; D013696:Temperature; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D002021:Buffers; D012492:Salts; D012996:Solutions; D014867:Water; D019346:Sodium Acetate; D009113:Muramidase; D005990:Glycerol; D006851:Hydrochloric Acid