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SANS studies of concentrated protein solutions. I. Bovine serum albumin
Author(s) -
Nossal R.,
Glinka C. J.,
Chen S.H.
Publication year - 1986
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360250613
Subject(s) - dlvo theory , chemistry , bovine serum albumin , ionic strength , neutron scattering , scattering , colloid , intermolecular force , chemical physics , small angle neutron scattering , crystallography , molecule , chromatography , physics , aqueous solution , organic chemistry , quantum mechanics
Small‐angle neutron scattering (SANS) was used to examine concentrated bovine serum albumin solutions of up to 20% protein w/v. At higher protein concentrations, scattering data show distinct features that can be ascribed to strong intermolecular interactions. Differential scattering cross‐sections are fitted to a theoretical model of interparticle potential consisting of a hard core plus an exponentially decaying “tail.” For moderate ionic strength (0.03 M K Acetate, pH 5.9), the intermolecular interaction agrees with the double‐layer repulsive part of the well‐known DLVO (Derjaguin, Landau, Verwey, Overbeek) theory for interacting colloidal particles. We thus demonstrate that it is possible to determine size parameters and the surface charge of protein molecules in dense solutions. At high salt concentrations (≥0.2 M NaCl) data can be fitted by the same potential model, although interpretation in terms of DLVO theory is not possible. Even in this case, however, “effective” molecular size and potential parameters can be determined.