SANS on lysozyme and lactoglobulin solutions

Giordano, R.; Grasso, Antonio; Teixeira, J.; Wanderlingh, U.

doi:10.1016/0921-4526(92)90459-6

Cited by 6 publications

(2 citation statements)

References 2 publications

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“…It is seen that in the low Q region of the SANS data, the scattering intensity increases with the increase in pH value of the solution. The monomer is a prolate ellipsoidal with dimensions a ¼ 22:0 A and b ¼ 13:5 A; being in good agreement with the previously reported results (14). The data were fitted using Eq.…”

Section: Small-angle Neutron Scattering Analysissupporting

confidence: 86%

Small-angle neutron scattering study of macromolecular aggregation in aqueous lysozyme solution

Seth¹,

Aswal²

2002

Journal of Macromolecular Science, Part B

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Small-angle neutron scattering measurements have been carried out to determine the state of macromolecular aggregation in undersaturated solutions of hen egg white lysozyme at different pH and with the addition of salt. These studies are of interest to understand the changes prior to protein crystallization in solution. It is found that macromolecular aggregation takes place with the change in pH or the salt concentration. Dimers are formed in the solution; the volume fraction of dimers increases with an increase in the pH or salt concentration. The combined effect of pH and salt is additive. 77

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Section: Small-angle Neutron Scattering Analysissupporting

confidence: 86%

Small-angle neutron scattering study of macromolecular aggregation in aqueous lysozyme solution

Seth¹,

Aswal²

2002

Journal of Macromolecular Science, Part B

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“…A protein of particular interest is hen egg lysozyme, which crystallizes readily and for which solubility and crystallization parameters are known. Some aspects of the interactions in lysozyme solutions have been studied separately by static light scattering (SLS) (George and Wilson, 1994;Muschol and Rosenberger, 1995;George et al, 1997), x-ray scattering (Ducruix et al, 1996), and small-angle neutron scattering (SANS) (Giordano et al, 1991(Giordano et al, , 1992Niimura et al, 1994;Gripon et al, 1996Gripon et al, , 1997. Scattering methods have also been applied in an attempt to characterize the size and the growth dynamics of the initial aggregates in the crystallization process (Boue et al, 1993;Niimura et al, 1995;Tanaka et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

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

Velev

Kaler

Lenhoff

1998

Biophysical Journal

330

443

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

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Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation

Sjöberg

Mortensen

1994

Biophysical Chemistry

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SANS on lysozyme and lactoglobulin solutions

Cited by 6 publications

References 2 publications

Small-angle neutron scattering study of macromolecular aggregation in aqueous lysozyme solution

Small-angle neutron scattering study of macromolecular aggregation in aqueous lysozyme solution

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

Interparticle interactions and structure in nonideal solutions of human serum albumin studied by small-angle neutron scattering and Monte Carlo simulation

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