Structure and interparticle interactions of bovine serum albumin in solution studied by small-angle neutron scattering

Journal Article · Thu Apr 28 00:00:00 EDT 1983 · J. Phys. Chem.; (United States)

DOI:https://doi.org/10.1021/j100232a003· OSTI ID:5296193

Bendedouch, D ^[1]; Chen, S H

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1. Brookhaven National Lab., Upton, NY

A series of small-angle neutron scattering (SANS) measurements were carried out on dilute and moderately concentrated bovine serum albumin (BSA) solutions at two different pH values and at t = 35/sup 0/C. The amount of bound water to the protein was deduced from the zero-contrast point of dilute BSA solutions, in D/sub 2/O and H/sub 2/O solvent mixtures. Detailed analysis of the intensity spectrum from the most dilute BSA solution in D/sub 2/O yields a prolate ellipsoidal shape (a,b,b) of the protein molecule with a = 70 angstrom and b = 20 angstrom. At moderate concentrations, pH 7, with or without salt (LiCl) added, the intensity spectra can be fitted satisfactorily by taking into account both the ellipsoidal shape of the particle and an interparticle interference factor (S(Q)). Calculation of S(Q) assumes a model of equivalent charged hard spheres interacting through a repulsive potential. For moderately concentrated solutions at pH 5.1, S(Q) can be accounted for by introducing an attractive potential between the particles.

• OSTI ID: 5296193
• Journal Information: J. Phys. Chem.; (United States), Vol. 87:9
• Country of Publication: United States
• Language: English

Related Subjects

63 RADIATION, THERMAL, AND OTHER ENVIRON. POLLUTANT EFFECTS ON LIVING ORGS. AND BIOL. MAT.
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NEUTRON SPECTRA
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LITHIUM CHLORIDES
MOLECULAR MODELS
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OXYGEN COMPOUNDS
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560111* - Radiation Effects on Biochemicals- In Vitro- (-1987)