Abstract
AbstractSmall‐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 (0.03M 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 (≥0.2M 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.
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Dates
Type | When |
---|---|
Created | 20 years, 8 months ago (Dec. 29, 2004, 9:01 p.m.) |
Deposited | 1 year, 10 months ago (Oct. 21, 2023, 8:40 p.m.) |
Indexed | 1 year ago (Aug. 30, 2024, 8:22 a.m.) |
Issued | 39 years, 2 months ago (June 1, 1986) |
Published | 39 years, 2 months ago (June 1, 1986) |
Published Online | 21 years, 6 months ago (Feb. 1, 2004) |
Published Print | 39 years, 2 months ago (June 1, 1986) |
@article{Nossal_1986, title={SANS studies of concentrated protein solutions. I. Bovine serum albumin}, volume={25}, ISSN={1097-0282}, url={http://dx.doi.org/10.1002/bip.360250613}, DOI={10.1002/bip.360250613}, number={6}, journal={Biopolymers}, publisher={Wiley}, author={Nossal, R. and Glinka, C. J. and Chen, S.‐H.}, year={1986}, month=jun, pages={1157–1175} }