Protein phase behavior and crystallization: Effect of glycerol

H. Sedgwick, J. E. Cameron, Wilson Poon, S. U. Egelhaaf

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article number125102
Pages (from-to)-
Number of pages6
JournalThe Journal of Chemical Physics
Volume127
Issue number12
DOIs
Publication statusPublished - 28 Sept 2007

Keywords / Materials (for Non-textual outputs)

  • LYSOZYME-LYSOZYME INTERACTIONS
  • 2ND VIRIAL-COEFFICIENTS
  • ORGANIC-SOLVENTS
  • DIELECTRIC-CONSTANTS
  • COLLOIDAL PARTICLES
  • CRYSTAL NUCLEATION
  • SOLUBILITY
  • WATER
  • CRYOPRESERVATION
  • THERMOSTABILITY

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