The solubility of hen egg-white lysozyme

Howard, Sandra B.; Twigg, Pamela D.; Baird, James K.; Meehan, Edward J.

doi:10.1016/0022-0248(88)90303-x

Cited by 200 publications

(139 citation statements)

References 22 publications

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“…We note that such an entropic attraction is not contained in DLVO theory. Its origin is also different from the salting out effect studied in [12,[57][58][59][60] or the macroion overcharging effect studied in [61]. In Figure 8 the salt dependence of the total interaction force F (r) (Eq.…”

Section: Microion Distributions Around a Single Proteinmentioning

confidence: 83%

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

et al. 2003

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The osmotic virial coefficient B 2 of globular protein solutions is calculated as a function of added salt concentration at fixed pH by computer simulations of the "primitive model". The salt and counter-ions as well as a discrete charge pattern on the protein surface are explicitly incorporated. For parameters roughly corresponding to lysozyme, we find that B 2 first decreases with added salt concentration up to a threshold concentration, then increases to a maximum, and then decreases again upon further raising the ionic strength.Our studies demonstrate that the existence of a discrete charge pattern on the protein surface profoundly influences the effective interactions and that nonlinear Poisson Boltzmann and Derjaguin-Landau-Verwey-Overbeek (DLVO) theory fail for large ionic strength. The observed non-monotonicity of B 2 is compared to experiments. Implications for protein crystallization are discussed.

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Section: Microion Distributions Around a Single Proteinmentioning

confidence: 83%

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

et al. 2003

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“…Over the last 15 years the solubility of lysozyme and in particular its tetragonal crystals has been studied by several groups, employing a variety of techniques (Ataka & Asai, 1988;Howard et al, 1988;Miyashita et al, 1993;Ries-Kautt & Ducruix, 1989;Rosenberger et al, 1993). Fortunately, in the areas of overlap, these techniques have produced rather consistent results, certifying to the accuracy of the determinations (Miyashita et al, 1993;Rosenberger et al, 1993).…”

Section: Lysozyme -Negative Crystallization Enthalpy and Entropymentioning

confidence: 99%

Solvent entropy contribution to the free energy of protein crystallization

Vekilov

Feeling-Taylor²,

Yau³

et al. 2002

Acta Crystallogr D Biol Crystallogr

102

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We show with three proteins that trapping and release of the water molecules upon crystallization is a determinant of the crystallization thermodynamics. With HbC, a strong retrograde solubility dependence on temperature yields a high positive enthalpy of 155 kJ mol -1 , i.e., crystallization is only possible because of the huge entropy gain of 610 J mol, stemming from the release of up to 10 water molecules per protein intermolecular contact. With apoferritin, the enthalpy of crystallization is close to zero. The main component in the crystallization driving force is the entropy gain due to the release upon crystallization of two water molecules bound to one protein molecules in solution. With both proteins, the density of the growth sites imaged by AFM is in excellent agreement with a calculation using the crystallization free energy. With lysozyme, the entropy effect due to the restructuring of the water molecules is negative. This leads to higher solubility.

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“…They were brought to supersaturation by adding NaCI to a final concentration of ~ 1998 International Union of ('rystallography Printed in Great Britain -all rights reserved 6% (w/v). Experimental data reported in the literature (Howard et al, 1988: Gripon et al, 1997 indicate a solubility of 4-6 mg ml-~ for lysozymc in an aqueous solution with 6% NaCI and pH 4.7 in the temperature range 293-303 K. The effect of D20 on the solubility is small (Gripon et al. 1997).…”

Section: Methodsmentioning

confidence: 98%

Nucleation in Protein Crystallization

Drenth

Haas

1998

Acta Crystallogr D Biol Crystallogr

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In this paper protein crystallization is regarded as a process starting with phase separation in a twocomponent system. The nucleation time of a lysozyme solution is measured by recording the NMR spectra of crystallizing solutions as a function of time. It is found that there is an appreciable induction time before the first nuclei appear in the solution and that this induction time depends strongly on the degree of supersaturation owing to the protein concentration at a given ionic strength or owing to the temperature. From the experimental data it is evident that (at least for lysozymc) crystallization under the prevailing experimental conditions is a transient process with an induction time and not a steady-state process.

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The solubility of hen egg-white lysozyme

Cited by 200 publications

References 22 publications

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Nonmonotonic variation with salt concentration of the second virial coefficient in protein solutions

Solvent entropy contribution to the free energy of protein crystallization

Nucleation in Protein Crystallization

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