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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 language | English |
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Article number | 125102 |
Pages (from-to) | - |
Number of pages | 6 |
Journal | The Journal of Chemical Physics |
Volume | 127 |
Issue number | 12 |
DOIs | |
Publication status | Published - 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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Dive into the research topics of 'Protein phase behavior and crystallization: Effect of glycerol'. Together they form a unique fingerprint.Projects
- 1 Finished
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Edinburgh Soft Matter and Statistical Physics Group: Programme Grant
Cates, M., Ackland, G., Egelhaaf, S., Evans, M., Poon, W. & Pusey, P.
1/10/03 → 31/03/08
Project: Research